SitesBLAST
Comparing H281DRAFT_05400 FitnessBrowser__Burk376:H281DRAFT_05400 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
8gy3C Cryo-em structure of membrane-bound aldehyde dehydrogenase from gluconobacter oxydans
29% identity, 89% coverage: 77:742/749 of query aligns to 15:718/732 of 8gy3C
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): M38 (= M100), G39 (= G101), Q40 (= Q102), H41 (≠ G103), V42 (= V104), A45 (≠ S107), G79 (= G146), G80 (= G147), S81 (= S148), S83 (= S150), V84 (≠ I151), G374 (= G427), F375 (= F428), L379 (= L432), L499 (vs. gap), R500 (= R545), V624 (= V648), D625 (≠ N649), Q632 (= Q656), T687 (≠ G711), G688 (= G712), L689 (≠ I713), G690 (= G714), E691 (= E715)
3hrdE Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 47% coverage: 224:575/749 of query aligns to 2:380/420 of 3hrdE
- active site: Q207 (= Q397), L242 (= L432), R318 (≠ D507), H322 (≠ A517), R350 (= R545)
- binding calcium ion: T206 (≠ S396), N208 (≠ V398), D212 (≠ V402), K241 (≠ R431), L242 (= L432), D243 (≠ E433)
- binding pterin cytosine dinucleotide: G237 (= G427), F238 (= F428), R350 (= R545)
- binding selenium atom: F238 (= F428), A348 (≠ F543), F349 (≠ W544), R350 (= R545)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 47% coverage: 224:575/749 of query aligns to 2:380/420 of 3hrdA
- active site: Q207 (= Q397), L242 (= L432), R318 (≠ D507), H322 (≠ A517), R350 (= R545)
- binding pterin cytosine dinucleotide: G236 (= G426), G237 (= G427), F238 (= F428), R350 (= R545)
- binding magnesium ion: T206 (≠ S396), N208 (≠ V398), D212 (≠ V402), K241 (≠ R431), L242 (= L432), D243 (≠ E433), T305 (≠ S495), Y308 (≠ M497), A309 (= A498), S346 (≠ T541)
- binding nicotinic acid: A314 (≠ P503), R318 (≠ D507), F352 (≠ V547)
- binding selenium atom: F238 (= F428), G239 (= G429), A348 (≠ F543), F349 (≠ W544), R350 (= R545)
Q0QLF2 Nicotinate dehydrogenase large molybdopterin subunit; NDH; Nicotinic acid hydroxylase large molybdopterin subunit; NAH; EC 1.17.1.5 from Eubacterium barkeri (Clostridium barkeri) (see 2 papers)
23% identity, 47% coverage: 224:575/749 of query aligns to 3:381/425 of Q0QLF2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:425 modified: mature protein, Nicotinate dehydrogenase large molybdopterin subunit
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
37% identity, 18% coverage: 608:742/749 of query aligns to 611:753/769 of O33819
- VGKALN 650:655 (≠ CGMVVN 644:649) binding
- KEAS 722:725 (vs. gap) binding
Sites not aligning to the query:
- 214 binding
- 244:245 binding
- 522:526 binding
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
37% identity, 18% coverage: 608:742/749 of query aligns to 603:745/761 of 1rm6A
- active site: E718 (= E715), G719 (≠ P716)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): L646 (≠ V648), N647 (= N649), V651 (= V653), Q654 (= Q656), K714 (vs. gap), E715 (vs. gap), A716 (vs. gap), S717 (vs. gap), E718 (= E715)
Sites not aligning to the query:
- active site: 206, 241, 318, 322, 350
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 235, 236, 237, 238, 350, 473, 474, 475, 476, 513, 514, 515, 517, 518
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
39% identity, 17% coverage: 618:742/749 of query aligns to 608:742/748 of 5y6qC
Sites not aligning to the query:
- active site: 204, 239, 310, 316, 344
- binding pterin cytosine dinucleotide: 233, 234, 235, 461, 462, 463, 464, 468, 500, 502, 503, 504, 505
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
25% identity, 47% coverage: 221:575/749 of query aligns to 9:380/732 of P77489
Sites not aligning to the query:
- 440 mutation R->H,K: Decrease in catalytic efficiency.
- 468:470 binding
- 511:512 binding
- 615:621 binding
- 625 binding
- 688:691 binding
- 692 E→Q: Loss of activity.
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
25% identity, 47% coverage: 221:575/749 of query aligns to 9:380/731 of 5g5gC
Sites not aligning to the query:
- active site: 692, 693
- binding pterin cytosine dinucleotide: 468, 469, 470, 507, 509, 511, 512, 617, 618, 621, 625, 688, 690, 691, 692
3hrdB Crystal structure of nicotinate dehydrogenase (see paper)
34% identity, 17% coverage: 618:742/749 of query aligns to 183:316/330 of 3hrdB
- active site: E289 (= E715), P290 (= P716)
- binding pterin cytosine dinucleotide: I215 (≠ V648), N216 (= N649), M219 (≠ T652), V220 (= V653), Q223 (= Q656), K285 (vs. gap), G286 (= G712), V287 (≠ I713), G288 (= G714), E289 (= E715)
Sites not aligning to the query:
Q0QLF1 Nicotinate dehydrogenase medium molybdopterin subunit; NDH; Nicotinic acid hydroxylase medium molybdopterin subunit; NAH; EC 1.17.1.5 from Eubacterium barkeri (Clostridium barkeri) (see paper)
34% identity, 17% coverage: 618:742/749 of query aligns to 183:316/330 of Q0QLF1
- 211:223 (vs. 644:656, 38% identical) binding
- AKGVGE 284:289 (≠ --GIGE 712:715) binding
Sites not aligning to the query:
- 45:49 binding
- 85:90 binding
Q8GUQ8 Xanthine dehydrogenase 1; AtXDH1; EC 1.17.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 46% coverage: 229:571/749 of query aligns to 598:967/1361 of Q8GUQ8
- E831 (≠ R431) mutation to A: Loss of activity.
- R909 (≠ V516) mutation to A: Decreases activity 12-fold.
Sites not aligning to the query:
- 364 W→A: Decreases activity 8-fold.
- 421 Y→A: Decreases activity 4-fold.
- 1297 E→A: Decreases activity 40-fold.
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
23% identity, 50% coverage: 207:581/749 of query aligns to 525:921/1295 of 6a7xA
- active site: Q740 (= Q397), E775 (≠ R431), R853 (≠ V516), H857 (vs. gap), R885 (= R545)
- binding bicarbonate ion: R812 (= R467), H813 (≠ P468), I850 (≠ A513), A883 (= A542), F884 (= F543), F887 (≠ V547), G888 (= G548), Q891 (≠ R551)
- binding uric acid: E775 (≠ R431), R853 (≠ V516), F887 (≠ V547)
Sites not aligning to the query:
- active site: 1233, 1234
- binding flavin-adenine dinucleotide: 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 314, 319, 322, 323, 325, 326, 332, 376
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 111, 113, 145, 147
- binding nicotinamide-adenine-dinucleotide: 329, 365, 366, 432, 433, 473, 480
- binding uric acid: 982, 983, 1052, 1234
P22985 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Rattus norvegicus (Rat) (see 2 papers)
23% identity, 50% coverage: 207:581/749 of query aligns to 552:948/1331 of P22985
Sites not aligning to the query:
- 43 binding
- 48 binding
- 51 binding
- 73 binding
- 112 binding
- 115 binding
- 147 binding
- 149 binding
- 256:263 binding
- 335:336 WF→AL: Converts the enzyme to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents.
- 346:350 binding
- 359 binding
- 403 binding
- 535 C→A: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with R-992. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with R-992 and S-1316.
- 992 C→R: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with A-535. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and S-1316.
- 1316 C→S: Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and R-992.
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
23% identity, 50% coverage: 207:581/749 of query aligns to 523:919/1291 of 6a7xB
- active site: Q738 (= Q397), E773 (≠ R431), R851 (≠ V516), H855 (vs. gap), R883 (= R545)
- binding bicarbonate ion: R810 (= R467), H811 (≠ P468), T880 (= T541), A881 (= A542), F885 (≠ V547), G886 (= G548), Q889 (≠ R551)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M376)
- binding uric acid: E773 (≠ R431), R851 (≠ V516), F885 (≠ V547)
Sites not aligning to the query:
- active site: 1231, 1232
- binding flavin-adenine dinucleotide: 44, 227, 228, 229, 230, 231, 232, 233, 234, 307, 312, 317, 320, 321, 323, 324, 330, 373, 374
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 111, 113, 145, 147
- binding nicotinamide-adenine-dinucleotide: 327, 363, 364, 428, 430, 431, 471, 478
- binding uric acid: 980, 981, 1049, 1050, 1232
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
23% identity, 50% coverage: 207:581/749 of query aligns to 525:921/1291 of 2e3tA
- active site: Q740 (= Q397), E775 (≠ R431), R853 (≠ V516), H857 (vs. gap), R885 (= R545)
- binding bicarbonate ion: R812 (= R467), H813 (≠ P468), I850 (≠ A513), T882 (= T541), A883 (= A542), F887 (≠ V547), G888 (= G548), Q891 (≠ R551)
- binding calcium ion: E713 (≠ A372), H714 (= H373), Y716 (≠ T375), T809 (≠ D464), G810 (≠ M465), G840 (≠ P503), T843 (≠ K506), E844 (≠ D507), S847 (≠ D510), S880 (vs. gap), N881 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L717 (≠ M376)
- binding uric acid: E775 (≠ R431), R853 (≠ V516), F887 (≠ V547)
Sites not aligning to the query:
- active site: 1233, 1234
- binding flavin-adenine dinucleotide: 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 318, 319, 322, 323, 325, 326, 331, 332, 375, 376
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 113, 145, 147
- binding uric acid: 982, 983, 1051, 1052, 1234
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
23% identity, 50% coverage: 207:581/749 of query aligns to 523:919/1286 of 4yswA
- active site: Q738 (= Q397), E773 (≠ R431), R851 (≠ V516), H855 (vs. gap), R883 (= R545)
- binding bicarbonate ion: R810 (= R467), H811 (≠ P468), I848 (≠ A513), T880 (= T541), A881 (= A542), F882 (= F543), F885 (≠ V547), G886 (= G548), Q889 (≠ R551)
- binding calcium ion: G838 (≠ P503), T841 (≠ K506), E842 (≠ D507), S845 (≠ D510), S878 (vs. gap), N879 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M376)
- binding uric acid: E773 (≠ R431), R851 (≠ V516), F885 (≠ V547)
Sites not aligning to the query:
- active site: 1231, 1232
- binding flavin-adenine dinucleotide: 44, 226, 227, 228, 229, 230, 231, 232, 233, 234, 307, 308, 312, 316, 317, 320, 321, 323, 324, 329, 330, 373, 374, 399
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 110, 111, 113, 145, 147
- binding 1,4-dihydronicotinamide adenine dinucleotide: 233, 326, 327, 328, 363, 364, 400, 401, 428, 430, 431, 471, 478, 1196
- binding uric acid: 980, 981, 1050, 1232
P47989 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Homo sapiens (Human) (see 4 papers)
23% identity, 50% coverage: 207:581/749 of query aligns to 553:949/1333 of P47989
- P555 (≠ A209) to S: in dbSNP:rs45577338
- D584 (≠ P239) to A: in dbSNP:rs45491693
- R607 (≠ A261) to Q: in dbSNP:rs45442092
- K617 (= K271) to N: in dbSNP:rs45442398
- T623 (≠ D277) to I: in dbSNP:rs45448694
- I646 (≠ A295) to V: in dbSNP:rs17323225
- I703 (≠ L334) to V: in dbSNP:rs17011368
- L763 (≠ I392) to F: in a breast cancer sample; somatic mutation
- R791 (≠ H420) to G: in a breast cancer sample; somatic mutation; dbSNP:rs775646772
- T910 (= T541) to M: in dbSNP:rs669884
Sites not aligning to the query:
- 133 E → K: in dbSNP:rs45447191
- 172 G → R: in dbSNP:rs45523133
- 235 T → M: in dbSNP:rs45469499
- 257:264 binding
- 337 binding
- 347:351 binding
- 360 binding
- 395 K → M: in dbSNP:rs34929837
- 422 binding
- 509 modified: Disulfide link with 1318, In oxidase form
- 536 modified: Disulfide link with 993, In oxidase form
- 993 modified: Disulfide link with 536, In oxidase form
- 1091 V → L: in dbSNP:rs45619033
- 1109 N → T: in dbSNP:rs45547640
- 1150 P → R: in dbSNP:rs1042036
- 1176 R → C: in dbSNP:rs45624433
- 1296 R → W: in dbSNP:rs45564939
- 1318 modified: Disulfide link with 509, In oxidase form
2e1qA Crystal structure of human xanthine oxidoreductase mutant, glu803val (see paper)
23% identity, 50% coverage: 207:581/749 of query aligns to 527:923/1307 of 2e1qA
- active site: Q742 (= Q397), V777 (≠ L432), R855 (≠ V516), H859 (vs. gap), R887 (= R545)
- binding bicarbonate ion: R814 (= R467), H815 (≠ P468), I852 (≠ A513), F886 (= F543), F889 (≠ V547), G890 (= G548), Q893 (≠ R551)
- binding calcium ion: E715 (≠ A372), H716 (= H373), Y718 (≠ T375), T741 (≠ S396), T747 (≠ V402), S780 (≠ F434), T781 (≠ D435), S784 (≠ T438), T811 (≠ D464), G812 (≠ M465)
- binding fe2/s2 (inorganic) cluster: L719 (≠ M376)
- binding hydroxy(dioxo)molybdenum: F773 (= F428), G774 (= G429), R887 (= R545)
Sites not aligning to the query:
- active site: 1235, 1236
- binding flavin-adenine dinucleotide: 43, 44, 230, 231, 232, 233, 234, 235, 236, 237, 238, 311, 312, 316, 320, 321, 324, 325, 327, 328, 333, 334, 377, 378
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 110, 111, 112, 114, 146, 148
- binding hydroxy(dioxo)molybdenum: 1053, 1054, 1236
2ckjA Human milk xanthine oxidoreductase
23% identity, 49% coverage: 216:581/749 of query aligns to 505:892/1264 of 2ckjA
Sites not aligning to the query:
- active site: 1204, 1205
- binding flavin-adenine dinucleotide: 228, 230, 231, 232, 233, 234, 308, 309, 317, 318, 321, 322, 324, 325, 331, 375
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 111, 112, 114, 146, 147, 148
Query Sequence
>H281DRAFT_05400 FitnessBrowser__Burk376:H281DRAFT_05400
MSQGLLDAQNGATSSPDASGKRGVSRRTFLKLSVTVGAAAGGGLLLGFSMPAVSQDQKAG
KSVIGGDANEAAQNGVFAPNAFIQIDTAGKVTLVIPKVEMGQGVYTSIPMLIAEELEVPL
DTVTLDHAPPDEKLFTDPLLGGQLTGGSTSIRYAWEPMRKAGATARMLLIGAAAQQWQVD
ASSCHAKSGQVIHAASNRSIGYGQLVDAAAKLPVPQNVPLKDPKDFKIIGTAVKRLDSPE
KVDGTATFGLDVRLPDMVYAAIANCPVFGGKLASVDDTNAKKIPGVRQVVKIDNAVAVIG
DHTWAAKRGLQALDIKWNEGADAKLSMKQIVDDLANASQRNGAVARKDGDVVHAFSNAKT
RVDAVYQQPFLAHATMEPINCTVHVRPDGCEIWLGSQVPTRVRDAAMAVTGLPADKIVVH
NHLIGGGFGRRLEFDMVTQAVKIGKQVSTPVKVLWTREEDIQHDMYRPYYYDKISAGLDA
NGKPLAWQHRIVGSSIMARFAPPAFKDGLDPDAVEVASDLPYDLPNQLVDYVRQEPHAIP
TAFWRGVGPTRGTFVVESFIDELAAEAKVDPVKYRRDLLGKTPRALNVLNTAAQAANWGS
AVPKGQGRGVSVMHAFGSYFAIVVDVAVDQGEVAVKRVVCAVDCGMVVNPNTVEAQVQGG
IIFGITAALYSEITIKDGRVEQNNFTDYRMLRIDETPPIDVHIVKSSEAPGGIGEPGTAA
LAPALTNAIFAATGKRLRQLPVGSQLKTA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory