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PaperBLAST

PaperBLAST Hits for sp|Q9HZF8|PYRD_PSEAE Dihydroorotate dehydrogenase (quinone) OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=pyrD PE=3 SV=1 (342 a.a., MYTLARQLLF...)

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Found 153 similar proteins in the literature:

PA3050 dihydroorotate dehydrogenase from Pseudomonas aeruginosa PAO1
100% identity, 100% coverage

PA14_24640 dihydroorotate dehydrogenase from Pseudomonas aeruginosa UCBPP-PA14
99% identity, 100% coverage

ACA40_10035 quinone-dependent dihydroorotate dehydrogenase from Pseudomonas syringae pv. lapsa
88% identity, 99% coverage

PSPPH_2077 dihydroorotate dehydrogenase from Pseudomonas syringae pv. phaseolicola 1448A
88% identity, 92% coverage

PsgB076_10315 quinone-dependent dihydroorotate dehydrogenase from Pseudomonas savastanoi pv. glycinea str. B076
87% identity, 99% coverage

BTH_I2511 dihydroorotate oxidase from Burkholderia thailandensis E264
61% identity, 97% coverage

B0V824 Dihydroorotate dehydrogenase (quinone) from Acinetobacter baumannii (strain AYE)
ABBFA_001187 dihydroorotate oxidase from Acinetobacter baumannii AB307-0294
59% identity, 98% coverage

VF_1285 dihydroorotate dehydrogenase 2 from Vibrio fischeri ES114
56% identity, 98% coverage

A6T739 Dihydroorotate dehydrogenase (quinone) from Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
57% identity, 98% coverage

7ut5A / B7GZW7 Acinetobacter baumannii dihydroorotate dehydrogenase bound with inhibitor dsm186 (see paper)
57% identity, 98% coverage

VC1491 dihydroorotate dehydrogenase from Vibrio cholerae O1 biovar eltor str. N16961
55% identity, 97% coverage

c1081 Dihydroorotate dehydrogenase from Escherichia coli CFT073
UTI89_C1010 dihydroorotate dehydrogenase from Escherichia coli UTI89
57% identity, 97% coverage

YPTB1439 dihydroorotate dehydrogenase from Yersinia pseudotuberculosis IP 32953
YPO1415 dihydroorotate dehydrogenase from Yersinia pestis CO92
55% identity, 98% coverage

A1S_2253 dihydroorotate dehydrogenase 2 from Acinetobacter baumannii ATCC 17978
63% identity, 85% coverage

PyrD / b0945 dihydroorotate dehydrogenase, type 2 (EC 1.3.5.2) from Escherichia coli K-12 substr. MG1655 (see 12 papers)
pyrD / P0A7E1 dihydroorotate dehydrogenase, type 2 (EC 1.3.5.2) from Escherichia coli (strain K12) (see 11 papers)
PYRD_ECOLI / P0A7E1 Dihydroorotate dehydrogenase (quinone); DHOdehase; DHOD; DHODase; Dihydroorotate oxidase; EC 1.3.5.2 from Escherichia coli (strain K12) (see 2 papers)
B1X8P9 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Escherichia coli (see paper)
1f76A / P0A7E1 Escherichia coli dihydroorotate dehydrogenase (see paper)
NP_415465 dihydroorotate dehydrogenase, type 2 from Escherichia coli str. K-12 substr. MG1655
b0945 dihydroorotate dehydrogenase from Escherichia coli str. K-12 substr. MG1655
ECs1029 dihydro-orotate dehydrogenase from Escherichia coli O157:H7 str. Sakai
57% identity, 98% coverage

ETAE_1248 dihydroorotate dehydrogenase 2 from Edwardsiella tarda EIB202
56% identity, 98% coverage

S1011 dihydro-orotate dehydrogenase from Shigella flexneri 2a str. 2457T
56% identity, 98% coverage

PMI_RS03790 quinone-dependent dihydroorotate dehydrogenase from Proteus mirabilis HI4320
55% identity, 98% coverage

t1862 dihydroorotate dehydrogenase from Salmonella enterica subsp. enterica serovar Typhi Ty2
55% identity, 98% coverage

STM1058 dihydro-orotate oxidase from Salmonella typhimurium LT2
55% identity, 98% coverage

BB3975 dihydroorotate dehydrogenase from Bordetella bronchiseptica RB50
56% identity, 96% coverage

NP_881968 dihydroorotate dehydrogenase from Bordetella pertussis Tohama I
BP3442 quinone-dependent dihydroorotate dehydrogenase from Bordetella pertussis Tohama I
55% identity, 96% coverage

Asuc_1385 Dihydroorotate oxidase from Actinobacillus succinogenes 130Z
53% identity, 98% coverage

HI1401 dihydroorotate dehydrogenase (pyrD) from Haemophilus influenzae Rd KW20
51% identity, 98% coverage

lpg1821 dihydroorotate oxidase from Legionella pneumophila subsp. pneumophila str. Philadelphia 1
51% identity, 87% coverage

BMEI1611 DIHYDROOROTATE DEHYDROGENASE from Brucella melitensis 16M
47% identity, 89% coverage

Caur_3923 Dihydroorotate oxidase from Chloroflexus aurantiacus J-10-fl
47% identity, 91% coverage

BOV_RS01655 quinone-dependent dihydroorotate dehydrogenase from Brucella ovis ATCC 25840
45% identity, 93% coverage

BAB1_0341 Dihydroorotate dehydrogenase:FMN/related compound-binding core:Dihydroorotate dehydrogenase 2 from Brucella melitensis biovar Abortus 2308
46% identity, 89% coverage

SCO1482 dihydroorotate dehydrogenase from Streptomyces coelicolor A3(2)
45% identity, 93% coverage

NP_001008608 dihydroorotate dehydrogenase (quinone), mitochondrial from Danio rerio
43% identity, 79% coverage

PYRD_RAT / Q63707 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Rattus norvegicus (Rat) (see 2 papers)
45% identity, 83% coverage

Q8NQC0 Dihydroorotate dehydrogenase (quinone) from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
cg1713 dihydroorotate dehydrogenase 2 from Corynebacterium glutamicum ATCC 13032
44% identity, 89% coverage

Q75XR0 dihydroorotate dehydrogenase (fumarate) (EC 1.3.98.1) from Euglena gracilis (see paper)
44% identity, 74% coverage

I7EMP0 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Phytophthora infestans (see paper)
PITG_01913 dihydroorotate dehydrogenase, mitochondrial precursor from Phytophthora infestans T30-4
43% identity, 78% coverage

PYRD_BOVIN / Q5E9W3 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Bos taurus (Bovine) (see 2 papers)
45% identity, 80% coverage

PYRD_HUMAN / Q02127 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Homo sapiens (Human) (see 5 papers)
Q02127 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Homo sapiens (see 11 papers)
NP_001352 dihydroorotate dehydrogenase (quinone), mitochondrial from Homo sapiens
44% identity, 83% coverage

9dhhA / Q02127 9dhhA (see paper)
44% identity, 89% coverage

LIC13433 dihydroorotate dehydrogenase from Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130
40% identity, 84% coverage

NP_064430 dihydroorotate dehydrogenase (quinone), mitochondrial precursor from Mus musculus
O35435 Dihydroorotate dehydrogenase (quinone), mitochondrial from Mus musculus
44% identity, 83% coverage

D2S350 Dihydroorotate dehydrogenase (quinone) from Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / 4k)
42% identity, 92% coverage

A8HZX8 Dihydroorotate dehydrogenase (quinone) from Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB 13405 / ORS 571)
45% identity, 92% coverage

SYNPCC7002_A2195 dihydroorotate dehydrogenase from Synechococcus sp. PCC 7002
42% identity, 84% coverage

4oriA / Q63707 Rat dihydroorotate dehydrogenase bound with dsm338 (n-[3,5-difluoro-4- (trifluoromethyl)phenyl]-5-methyl-2-(trifluoromethyl)[1,2, 4]triazolo[1,5-a]pyrimidin-7-amine) (see paper)
43% identity, 92% coverage

B7PXW4 Dihydroorotate dehydrogenase (quinone), mitochondrial (Fragment) from Ixodes scapularis
41% identity, 88% coverage

XP_004924203 dihydroorotate dehydrogenase (quinone), mitochondrial isoform X2 from Bombyx mori
40% identity, 85% coverage

Rv2139 dihydroorotate dehydrogenase from Mycobacterium tuberculosis H37Rv
43% identity, 94% coverage

CSUI_008592 dihydroorotate dehydrogenase from Cystoisospora suis
39% identity, 51% coverage

XP_794275 dihydroorotate dehydrogenase (quinone), mitochondrial from Strongylocentrotus purpuratus
41% identity, 80% coverage

MSMEG_4198 dihydroorotate oxidase from Mycobacterium smegmatis str. MC2 155
45% identity, 83% coverage

slr1418 dihydroorotate dehydrogenase from Synechocystis sp. PCC 6803
41% identity, 80% coverage

6ajeA / U6KL66 Crystal structure of dhodh in complex with ferulenol from eimeria tenella (see paper)
41% identity, 85% coverage

M1BCR0 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Solanum tuberosum (see paper)
40% identity, 69% coverage

SAUSA300_2526 dihydroorotate dehydrogenase from Staphylococcus aureus subsp. aureus USA300_FPR3757
SACOL2606 dihydroorotate dehydrogenase from Staphylococcus aureus subsp. aureus COL
38% identity, 95% coverage

SAPIG2639 quinone-dependent dihydroorotate dehydrogenase from Staphylococcus aureus subsp. aureus ST398
37% identity, 95% coverage

SA2375 dihydroorotate dehydrogenase from Staphylococcus aureus subsp. aureus N315
37% identity, 95% coverage

PYRD / P32746 dihydroorotate dehydrogenase (EC 1.3.5.2) from Arabidopsis thaliana (see 2 papers)
PYRD_ARATH / P32746 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
P32746 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Arabidopsis thaliana (see paper)
AT5G23300 PYRD (pyrimidine d); dihydroorotate dehydrogenase from Arabidopsis thaliana
39% identity, 72% coverage

SAR2669 putative dihydroorotate dehydrogenase from Staphylococcus aureus subsp. aureus MRSA252
37% identity, 95% coverage

U6KL66 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Eimeria tenella (see paper)
XP_013227840 dihydroorotate dehydrogenase, putative from Eimeria tenella
39% identity, 78% coverage

Q7XKC8 Dihydroorotate dehydrogenase (quinone), mitochondrial from Oryza sativa subsp. japonica
37% identity, 69% coverage

B6U892 Dihydroorotate dehydrogenase (quinone), mitochondrial from Zea mays
NP_001152058 dihydroorotate dehydrogenase from Zea mays
37% identity, 69% coverage

8ofwA / P9WHL1 Crystal structure of the full-length dihydroorotate dehydrogenase from mycobacterium tuberculosis (see paper)
42% identity, 95% coverage

K3ZE81 Dihydroorotate dehydrogenase (quinone), mitochondrial from Setaria italica
37% identity, 71% coverage

Q8MXD1 dihydroorotate dehydrogenase (fumarate) (EC 1.3.98.1) from Toxoplasma gondii (see paper)
TGME49_210790, XP_002371234 dihydroorotate dehydrogenase reveal, putative from Toxoplasma gondii ME49
38% identity, 55% coverage

PYRD_SCHPO / P32747 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOD; DHODase; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 3 papers)
ura3 / RF|NP_593317.1 dihydroorotate dehydrogenase Ura3; EC 1.3.3.1 from Schizosaccharomyces pombe (see paper)
NP_593317, SPAC57A10.12c dihydroorotate dehydrogenase Ura3 from Schizosaccharomyces pombe
38% identity, 73% coverage

G8BA68 Dihydroorotate dehydrogenase (quinone), mitochondrial from Candida parapsilosis (strain CDC 317 / ATCC MYA-4646)
CPAR2_804900 uncharacterized protein from Candida parapsilosis
39% identity, 68% coverage

G4VFD7 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Schistosoma mansoni (see 2 papers)
XP_018651255 dihydroorotate dehydrogenase from Schistosoma mansoni
40% identity, 85% coverage

6uy4A / G4VFD7 Crystal structure of dihydroorotate dehydrogenase from schistosoma mansoni (see paper)
39% identity, 92% coverage

HVO_2943 dihydroorotate oxidase from Haloferax volcanii DS2
39% identity, 94% coverage

PBANKA_010210 dihydroorotate dehydrogenase, putative from Plasmodium berghei ANKA
37% identity, 61% coverage

PYRD_LACK1 / Q6V3W9 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOD; DHODase; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri) (see paper)
40% identity, 66% coverage

7l01B / Q08210 Crystal structure of plasmodium falciparum dihydroorotate dehydrogenase bound with inhibitor dsm782 (n-(1-(5-cyano-1h-pyrazol- 3-yl)ethyl)-3-methyl-4-(1-(6-(trifluoromethyl)pyridin-3-yl) cyclopropyl)-1h-pyrrole-2-carboxamide) (see paper)
40% identity, 71% coverage

PCHAS_0102800 dihydroorotate dehydrogenase, putative from Plasmodium chabaudi chabaudi
39% identity, 60% coverage

HP1011 dihydroorotate dehydrogenase (pyrD) from Helicobacter pylori 26695
35% identity, 97% coverage

CNAG_02794 dihydroorotate dehydrogenase (fumarate) from Cryptococcus neoformans var. grubii H99
37% identity, 60% coverage

W1QJ07 Dihydroorotate dehydrogenase (quinone), mitochondrial from Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
38% identity, 74% coverage

Q6SZS6 Dihydroorotate dehydrogenase (quinone), mitochondrial from Kluyveromyces marxianus
38% identity, 74% coverage

PYRD_CANAL / Q874I4 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOD; DHODase; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) (see paper)
Q874I4 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Candida albicans (see paper)
URA1 / GB|AAO74621.1 dihydroorotate dehydrogenase, mitochondrial (DHOdehase) (DHODase) (DHOD); EC 1.3.5.2 from Candida albicans (see paper)
37% identity, 74% coverage

PVX_113330 dihydroorotate dehydrogenase, mitochondrial precursor, putative from Plasmodium vivax
35% identity, 57% coverage

Q5KK62 Dihydroorotate dehydrogenase (quinone), mitochondrial from Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)
37% identity, 61% coverage

PYRD_PLAF7 / Q08210 Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; Dihydroorotate oxidase; EC 1.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
Q08210 dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) from Plasmodium falciparum (see 10 papers)
PF3D7_0603300, XP_966023 dihydroorotate dehydrogenase from Plasmodium falciparum 3D7
36% identity, 48% coverage

PCYB_115310 dihydroorotate dehydrogenase mitochondrial precursor from Plasmodium cynomolgi strain B
35% identity, 82% coverage

B6JXQ5 Dihydroorotate dehydrogenase (quinone), mitochondrial from Schizosaccharomyces japonicus (strain yFS275 / FY16936)
36% identity, 73% coverage

6b8sB / B5Z6I2 Crystal structure of dihydroorotate dehydrogenase from helicobacter pylori with bound fmn
34% identity, 100% coverage

F0UDX1 Orotate reductase from Ajellomyces capsulatus (strain H88)
32% identity, 57% coverage

Pc22g21410 uncharacterized protein from Penicillium rubens
30% identity, 58% coverage

AFUA_2G11010, Afu2g11010 dihydroorotate reductase PyrE, putative from Aspergillus fumigatus Af293
Q4X169 Dihydroorotate dehydrogenase (quinone), mitochondrial from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
31% identity, 53% coverage

BLGT_RS02540 quinone-dependent dihydroorotate dehydrogenase from Bifidobacterium longum subsp. longum GT15
30% identity, 88% coverage

pyrE dihydroorotate dehydrogenase; EC 1.3.1.14 from Emericella nidulans (see 2 papers)
Q12610 Dihydroorotate dehydrogenase (quinone), mitochondrial from Emericella nidulans
33% identity, 51% coverage

BBMN68_979 quinone-dependent dihydroorotate dehydrogenase from Bifidobacterium longum subsp. longum BBMN68
30% identity, 88% coverage

IHV18_09925 quinone-dependent dihydroorotate dehydrogenase from Bifidobacterium breve
29% identity, 88% coverage

MGG_08814 dihydroorotate dehydrogenase from Pyricularia oryzae 70-15
29% identity, 62% coverage

R1EHA9 Dihydroorotate dehydrogenase from Emiliania huxleyi
29% identity, 68% coverage

DET1372 dihydroorotate dehydrogenase from Dehalococcoides ethenogenes 195
31% identity, 85% coverage

PYRDB_DESRM / A4J560 Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit; DHOD B; DHODase B; DHOdehase B; Dihydroorotate oxidase B; Orotate reductase (NADH); EC 1.3.1.14 from Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1) (Desulfotomaculum reducens) (see paper)
Dred_1686 dihydroorotate dehydrogenase family protein from Desulfotomaculum reducens MI-1
30% identity, 80% coverage

TDE0982 dihydroorotate dehydrogenase/oxidoreductase, FAD-binding from Treponema denticola ATCC 35405
26% identity, 41% coverage

LM6179_2603 dihydroorotate dehydrogenase from Listeria monocytogenes 6179
27% identity, 87% coverage

Q7Z892 Dihydroorotate dehydrogenase (fumarate) from Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651)
26% identity, 88% coverage

pyrD / P25996 dihydroorotate dehydrogenase (catalytic subunit) (EC 1.3.1.14) from Bacillus subtilis (strain 168) (see 2 papers)
PYRDB_BACSU / P25996 Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit; DHOD B; DHODase B; DHOdehase B; Dihydroorotate oxidase B; Orotate reductase (NADH); EC 1.3.1.14 from Bacillus subtilis (strain 168) (see paper)
pyrD / GB|CAB13428.1 dihydroorotate oxidase, catalytic subunit; EC 1.3.3.1 from Bacillus subtilis (see paper)
BSU15540 dihydroorotate dehydrogenase 1B from Bacillus subtilis subsp. subtilis str. 168
26% identity, 84% coverage

lmo1833 highly similar to dihydroorotase dehydrogenase from Listeria monocytogenes EGD-e
27% identity, 87% coverage

LBA1384 dihydroorotate dehydrogenase B, catalytic unit from Lactobacillus acidophilus NCFM
27% identity, 79% coverage

LOTGIDRAFT_233044 hypothetical protein from Lottia gigantea
27% identity, 29% coverage

B5X54_RS07485 dihydroorotate dehydrogenase from Caldicellulosiruptor bescii
27% identity, 85% coverage

CS401_RS10030 dihydroorotate dehydrogenase from Fusobacterium vincentii
26% identity, 80% coverage

PYRDB_ENTFA / P0DH74 Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit; DHOD B; DHODase B; DHOdehase B; Dihydroorotate oxidase B; Orotate reductase (NADH); EC 1.3.1.14 from Enterococcus faecalis (strain ATCC 700802 / V583) (see paper)
EF1714 dihydroorotate dehydrogenase from Enterococcus faecalis V583
25% identity, 87% coverage

URA1 / P28272 dihydroorotate dehydrogenase subunit (EC 1.3.98.1) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (see 3 papers)
PYRD_YEAST / P28272 Dihydroorotate dehydrogenase (fumarate); DHOD; DHODase; DHOdehase; Dihydroorotate oxidase; EC 1.3.98.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 7 papers)
NP_012706 dihydroorotate dehydrogenase from Saccharomyces cerevisiae S288C
NP_012706, YKL216W Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid from Saccharomyces cerevisiae
26% identity, 80% coverage

CAC2650 Dihydroorotate dehydrogenase from Clostridium acetobutylicum ATCC 824
26% identity, 79% coverage

B7X933 dihydroorotate dehydrogenase (NAD+) (EC 1.3.1.14) from Bifidobacterium bifidum (see paper)
28% identity, 83% coverage

2b4gB / Q57U83 Dihydroorotate dehydrogenase (see paper)
26% identity, 84% coverage

pyrDB / Q9CFW8 dihydroorotate dehydrogenase, catalytic subunit (EC 1.3.1.14) from Lactococcus lactis subsp. lactis (strain IL1403) (see 6 papers)
29% identity, 80% coverage

PYRD_TRYB2 / Q57U83 Dihydroorotate dehydrogenase (fumarate); DHOD; DHODase; DHOdehase; Dihydroorotate oxidase; EC 1.3.98.1 from Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (see paper)
XP_845053 dihydroorotate dehydrogenase, putative from Trypanosoma brucei brucei TREU927
28% identity, 84% coverage

BC3884 Dihydroorotate dehydrogenase, catalytic subunit from Bacillus cereus ATCC 14579
26% identity, 84% coverage

LSA0446 Putative dihydroorotate oxidase, catalytic subunit from Lactobacillus sakei subsp. sakei 23K
24% identity, 84% coverage

NP_727320 suppressor of rudimentary from Drosophila melanogaster
26% identity, 29% coverage

D2V5Y1 dihydropyrimidine dehydrogenase (NADP(+)) from Naegleria gruberi
26% identity, 28% coverage

Q8CHR6 Dihydropyrimidine dehydrogenase [NADP(+)] from Mus musculus
27% identity, 29% coverage

Dpyd / O89000 dihydropyrimidine dehydrogenase monomer (EC 1.3.1.2) from Rattus norvegicus (see 3 papers)
O89000 Dihydropyrimidine dehydrogenase [NADP(+)] from Rattus norvegicus
26% identity, 29% coverage

BAD_RS04070 dihydroorotate dehydrogenase from Bifidobacterium adolescentis ATCC 15703
28% identity, 84% coverage

Q80XT4 Dihydropyrimidine dehydrogenase [NADP(+)] (Fragment) from Mus musculus
27% identity, 34% coverage

XP_003722973 dihydroorotate dehydrogenase from Leishmania braziliensis MHOM/BR/75/M2904
27% identity, 86% coverage

Q8DTV0 Dihydroorotate dehydrogenase from Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
27% identity, 78% coverage

LCA_RS04790 dihydroorotate dehydrogenase from Latilactobacillus sakei subsp. sakei 23K
26% identity, 86% coverage

I3U217 dihydroorotate oxidase (fumarate) from Enterococcus faecium (strain ATCC BAA-472 / TX0016 / DO)
25% identity, 74% coverage

XP_025008718 dihydropyrimidine dehydrogenase [NADP(+)] isoform X3 from Gallus gallus
27% identity, 30% coverage

SGRA_p0002 dihydroorotate oxidase from Saprospira grandis str. Lewin
24% identity, 79% coverage

DPYD / Q12882 Dihydropyrimidine dehydrogenase [NADP+] (EC 1.3.1.2) from Homo sapiens (see 3 papers)
DPYD_HUMAN / Q12882 Dihydropyrimidine dehydrogenase [NADP(+)]; DHPDHase; DPD; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase; EC 1.3.1.2 from Homo sapiens (Human) (see 5 papers)
24% identity, 29% coverage

SUB1264 dihydroorotate dehydrogenase from Streptococcus uberis 0140J
25% identity, 74% coverage

DPYD_PIG / Q28943 Dihydropyrimidine dehydrogenase [NADP(+)]; DHPDHase; DPD; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase; EC 1.3.1.2 from Sus scrofa (Pig) (see 5 papers)
Q28943 dihydropyrimidine dehydrogenase (NADP+) (EC 1.3.1.2) from Sus scrofa (see 4 papers)
NP_999209 dihydropyrimidine dehydrogenase [NADP(+)] precursor from Sus scrofa
26% identity, 29% coverage

Q4DGV2 dihydroorotate dehydrogenase (fumarate) (EC 1.3.98.1) from Trypanosoma cruzi (see paper)
DHOD3 / GI|81295309 dihydroorotate dehydrogenase; EC 1.3.5.2 from Trypanosoma cruzi (see 2 papers)
25% identity, 88% coverage

SP70585_1004 dihydroorotate dehydrogenase B, catalytic subunit (dihydroorotate oxidase b) (dhodehase b) (dhodase b) (dhod b) from Streptococcus pneumoniae 70585
28% identity, 80% coverage

1gthA / Q28943 Dihydropyrimidine dehydrogenase (dpd) from pig, ternary complex with NADPH and 5-iodouracil (see paper)
26% identity, 29% coverage

3c61A / D0VWT2 Crystal structure of dihydroorotate dehydrogenase from leishmania donovani
26% identity, 86% coverage

SP_0964 dihydroorotate dehydrogenase 1B from Streptococcus pneumoniae TIGR4
SPCG_RS04890 dihydroorotate dehydrogenase from Streptococcus pneumoniae CGSP14
28% identity, 80% coverage

spr0866 dihydroorotate dehydrogenase 1B from Streptococcus pneumoniae R6
SPD_0852 dihydroorotate dehydrogenase, catalytic subunit from Streptococcus pneumoniae D39
28% identity, 80% coverage

pyrD / CAA91006.2 dihydroorotate dehydrogenase from Lactobacillus plantarum (see 2 papers)
P77887 Dihydroorotate dehydrogenase A (fumarate) from Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
lp_2699 dihydroorotate oxidase from Lactobacillus plantarum WCFS1
28% identity, 87% coverage

DPYD_CAEEL / Q18164 Dihydropyrimidine dehydrogenase [NADP(+)]; DHPDHase; DPD; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase; EC 1.3.1.2 from Caenorhabditis elegans (see paper)
26% identity, 27% coverage

XP_005270619 dihydropyrimidine dehydrogenase [NADP(+)] isoform X2 from Homo sapiens
28% identity, 18% coverage

DPYD_BOVIN / Q28007 Dihydropyrimidine dehydrogenase [NADP(+)]; DHPDHase; DPD; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase; EC 1.3.1.2 from Bos taurus (Bovine) (see paper)
30% identity, 17% coverage

LOC410207 dihydropyrimidine dehydrogenase [NADP(+)] from Apis mellifera
23% identity, 29% coverage

EF0285 dihydroorotate dehydrogenase from Enterococcus faecalis V583
27% identity, 72% coverage

PYRDA_LACLM / A2RJT9 Dihydroorotate dehydrogenase A (fumarate); DHOD A; DHODase A; DHOdehase A; EC 1.3.98.1 from Lactococcus lactis subsp. cremoris (strain MG1363) (see 4 papers)
A2RJT9 dihydroorotate dehydrogenase (NAD+) (EC 1.3.1.14) from Lactococcus lactis (see paper)
2bslA / A2RJT9 Crystal structure of l. Lactis dihydroorotate dehydrogense a in complex with 3,4-dihydroxybenzoate (see paper)
25% identity, 74% coverage

Q6F4D1 dihydroorotate dehydrogenase (fumarate) (EC 1.3.98.1) from Neobodo saliens (see paper)
26% identity, 46% coverage

L192589 dihydroorotate dehydrogenase A (EC 1.3.3.1) from Lactococcus lactis subsp. lactis Il1403
24% identity, 74% coverage

SPy_1432 dihydroorotate oxidase from Streptococcus pyogenes M1 GAS
SPy1432 putative dihydroorotate dehydrogenase from Streptococcus pyogenes M1 GAS
25% identity, 73% coverage

M28_Spy1159 dihydroorotate dehydrogenase from Streptococcus pyogenes MGAS6180
25% identity, 73% coverage

CD630_01860, CDIF630erm_00307 dihydroorotate dehydrogenase from Clostridioides difficile
25% identity, 87% coverage

gbs0553 unknown from Streptococcus agalactiae NEM316
26% identity, 84% coverage

PF1539 dihydroorotate dehydrogenase (dihydroorotate oxidase) (dhodehase) from Pyrococcus furiosus DSM 3638
24% identity, 86% coverage

Q8DVA1 dihydroorotate dehydrogenase (fumarate) (EC 1.3.98.1) from Streptococcus mutans (see paper)
25% identity, 74% coverage

3oixA / Q8DVA1 Crystal structure of the putative dihydroorotate dehydrogenase from streptococcus mutans (see paper)
25% identity, 74% coverage

Q5L029 dihydrouracil dehydrogenase (NAD(+)) from Geobacillus kaustophilus (strain HTA426)
28% identity, 33% coverage

pydA / Q846U6 (NADP)-dependent dihydropyrimidine dehydrogenase (EC 1.3.1.2) from Brevibacillus agri (see paper)
Q846U6 dihydrouracil dehydrogenase (NAD(+)) from Brevibacillus agri
25% identity, 39% coverage

Ac3H11_2954 Dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) from Acidovorax sp. GW101-3H11
27% identity, 39% coverage

New Search

For advice on how to use these tools together, see Interactive tools for functional annotation of bacterial genomes.

Statistics

The PaperBLAST database links 793,807 different protein sequences to 1,259,118 scientific articles. Searches against EuropePMC were last performed on March 13 2025.

How It Works

PaperBLAST builds a database of protein sequences that are linked to scientific articles. These links come from automated text searches against the articles in EuropePMC and from manually-curated information from GeneRIF, UniProtKB/Swiss-Prot, BRENDA, CAZy (as made available by dbCAN), BioLiP, CharProtDB, MetaCyc, EcoCyc, TCDB, REBASE, the Fitness Browser, and a subset of the European Nucleotide Archive with the /experiment tag. Given this database and a protein sequence query, PaperBLAST uses protein-protein BLAST to find similar sequences with E < 0.001.

To build the database, we query EuropePMC with locus tags, with RefSeq protein identifiers, and with UniProt accessions. We obtain the locus tags from RefSeq or from MicrobesOnline. We use queries of the form "locus_tag AND genus_name" to try to ensure that the paper is actually discussing that gene. Because EuropePMC indexes most recent biomedical papers, even if they are not open access, some of the links may be to papers that you cannot read or that our computers cannot read. We query each of these identifiers that appears in the open access part of EuropePMC, as well as every locus tag that appears in the 500 most-referenced genomes, so that a gene may appear in the PaperBLAST results even though none of the papers that mention it are open access. We also incorporate text-mined links from EuropePMC that link open access articles to UniProt or RefSeq identifiers. (This yields some additional links because EuropePMC uses different heuristics for their text mining than we do.)

For every article that mentions a locus tag, a RefSeq protein identifier, or a UniProt accession, we try to select one or two snippets of text that refer to the protein. If we cannot get access to the full text, we try to select a snippet from the abstract, but unfortunately, unique identifiers such as locus tags are rarely provided in abstracts.

PaperBLAST also incorporates manually-curated protein functions:

Except for GeneRIF and ENA, the curated entries include a short curated description of the protein's function. For entries from BioLiP, the protein's function may not be known beyond binding to the ligand. Many of these entries also link to articles in PubMed.

For more information see the PaperBLAST paper (mSystems 2017) or the code. You can download PaperBLAST's database here.

Changes to PaperBLAST since the paper was written:

Many of these changes are described in Interactive tools for functional annotation of bacterial genomes.

Secrets

PaperBLAST cannot provide snippets for many of the papers that are published in non-open-access journals. This limitation applies even if the paper is marked as "free" on the publisher's web site and is available in PubmedCentral or EuropePMC. If a journal that you publish in is marked as "secret," please consider publishing elsewhere.

Omissions from the PaperBLAST Database

Many important articles are missing from PaperBLAST, either because the article's full text is not in EuropePMC (as for many older articles), or because the paper does not mention a protein identifier such as a locus tag, or because of PaperBLAST's heuristics. If you notice an article that characterizes a protein's function but is missing from PaperBLAST, please notify the curators at UniProt or add an entry to GeneRIF. Entries in either of these databases will eventually be incorporated into PaperBLAST. Note that to add an entry to UniProt, you will need to find the UniProt identifier for the protein. If the protein is not already in UniProt, you can ask them to create an entry. To add an entry to GeneRIF, you will need an NCBI Gene identifier, but unfortunately many prokaryotic proteins in RefSeq do not have corresponding Gene identifers.

References

PaperBLAST: Text-mining papers for information about homologs.
M. N. Price and A. P. Arkin (2017). mSystems, 10.1128/mSystems.00039-17.

Europe PMC in 2017.
M. Levchenko et al (2017). Nucleic Acids Research, 10.1093/nar/gkx1005.

Gene indexing: characterization and analysis of NLM's GeneRIFs.
J. A. Mitchell et al (2003). AMIA Annu Symp Proc 2003:460-464.

UniProt: the universal protein knowledgebase.
The UniProt Consortium (2016). Nucleic Acids Research, 10.1093/nar/gkw1099.

BRENDA in 2017: new perspectives and new tools in BRENDA.
S. Placzek et al (2017). Nucleic Acids Research, 10.1093/nar/gkw952.

The EcoCyc database: reflecting new knowledge about Escherichia coli K-12.
I. M. Keeseler et al (2016). Nucleic Acids Research, 10.1093/nar/gkw1003.

The MetaCyc database of metabolic pathways and enzymes.
R. Caspi et al (2018). Nucleic Acids Research, 10.1093/nar/gkx935.

CharProtDB: a database of experimentally characterized protein annotations.
R. Madupu et al (2012). Nucleic Acids Research, 10.1093/nar/gkr1133.

The carbohydrate-active enzymes database (CAZy) in 2013.
V. Lombard et al (2014). Nucleic Acids Research, 10.1093/nar/gkt1178.

The Transporter Classification Database (TCDB): recent advances
M. H. Saier, Jr. et al (2016). Nucleic Acids Research, 10.1093/nar/gkv1103.

REBASE - a database for DNA restriction and modification: enzymes, genes and genomes.
R. J. Roberts et al (2015). Nucleic Acids Research, 10.1093/nar/gku1046.

Deep annotation of protein function across diverse bacteria from mutant phenotypes.
M. N. Price et al (2016). bioRxiv, 10.1101/072470.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory