SitesBLAST
Comparing BPHYT_RS24635 FitnessBrowser__BFirm:BPHYT_RS24635 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8gy3C Cryo-em structure of membrane-bound aldehyde dehydrogenase from gluconobacter oxydans
28% identity, 89% coverage: 73:743/750 of query aligns to 10:718/732 of 8gy3C
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): M38 (= M101), G39 (= G102), Q40 (= Q103), H41 (≠ G104), V42 (= V105), A45 (≠ S108), G79 (= G147), G80 (= G148), S81 (= S149), S83 (= S151), V84 (≠ I152), G374 (= G428), F375 (= F429), L379 (= L433), L499 (≠ W545), R500 (= R546), V624 (= V649), D625 (≠ N650), Q632 (= Q657), T687 (≠ G712), G688 (= G713), L689 (≠ I714), G690 (= G715), E691 (= E716)
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, 52% coverage: 225:614/750 of query aligns to 3:419/425 of Q0QLF2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:425 modified: mature protein, Nicotinate dehydrogenase large molybdopterin subunit
3hrdE Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 52% coverage: 225:614/750 of query aligns to 2:418/420 of 3hrdE
- active site: Q207 (= Q398), L242 (= L433), R318 (≠ N508), H322 (≠ A518), R350 (= R546)
- binding calcium ion: T206 (≠ S397), N208 (≠ V399), D212 (≠ V403), K241 (≠ R432), L242 (= L433), D243 (≠ E434)
- binding pterin cytosine dinucleotide: G237 (= G428), F238 (= F429), R350 (= R546)
- binding selenium atom: F238 (= F429), A348 (≠ F544), F349 (≠ W545), R350 (= R546)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 52% coverage: 225:614/750 of query aligns to 2:418/420 of 3hrdA
- active site: Q207 (= Q398), L242 (= L433), R318 (≠ N508), H322 (≠ A518), R350 (= R546)
- binding pterin cytosine dinucleotide: G236 (= G427), G237 (= G428), F238 (= F429), R350 (= R546)
- binding magnesium ion: T206 (≠ S397), N208 (≠ V399), D212 (≠ V403), K241 (≠ R432), L242 (= L433), D243 (≠ E434), T305 (≠ S496), Y308 (≠ M498), A309 (= A499), S346 (≠ T542)
- binding nicotinic acid: A314 (≠ P504), R318 (≠ N508), F352 (≠ V548)
- binding selenium atom: F238 (= F429), G239 (= G430), A348 (≠ F544), F349 (≠ W545), R350 (= R546)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
36% identity, 18% coverage: 609:743/750 of query aligns to 611:753/769 of O33819
- VGKALN 650:655 (≠ CGMVVN 645:650) 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)
36% identity, 18% coverage: 609:743/750 of query aligns to 603:745/761 of 1rm6A
- active site: E718 (= E716), G719 (≠ P717)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): L646 (≠ V649), N647 (= N650), V651 (≠ I654), Q654 (= Q657), K714 (vs. gap), E715 (vs. gap), A716 (vs. gap), S717 (vs. gap), E718 (= E716)
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
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
26% identity, 47% coverage: 222:576/750 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
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
26% identity, 47% coverage: 222:576/750 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.
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
36% identity, 17% coverage: 619:743/750 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
3hrdB Crystal structure of nicotinate dehydrogenase (see paper)
33% identity, 16% coverage: 625:743/750 of query aligns to 191:316/330 of 3hrdB
- active site: E289 (= E716), P290 (= P717)
- binding pterin cytosine dinucleotide: I215 (≠ V649), N216 (= N650), M219 (≠ T653), V220 (≠ I654), Q223 (= Q657), K285 (vs. gap), G286 (= G713), V287 (≠ I714), G288 (= G715), E289 (= E716)
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)
33% identity, 16% coverage: 625:743/750 of query aligns to 191:316/330 of Q0QLF1
- 211:223 (vs. 645:657, 31% identical) binding
- AKGVGE 284:289 (≠ --GIGE 713:716) binding
Sites not aligning to the query:
- 45:49 binding
- 85:90 binding
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
24% identity, 47% coverage: 216:565/750 of query aligns to 525:902/1291 of 6a7xB
- active site: Q738 (= Q398), E773 (≠ R432), R851 (≠ V517), H855 (vs. gap), R883 (= R546)
- binding bicarbonate ion: R810 (= R468), H811 (≠ P469), T880 (= T542), A881 (= A543), F885 (≠ V548), G886 (= G549), Q889 (≠ R552)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M377)
- binding uric acid: E773 (≠ R432), R851 (≠ V517), F885 (≠ V548)
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)
24% identity, 47% coverage: 216:565/750 of query aligns to 527:904/1291 of 2e3tA
- active site: Q740 (= Q398), E775 (≠ R432), R853 (≠ V517), H857 (vs. gap), R885 (= R546)
- binding bicarbonate ion: R812 (= R468), H813 (≠ P469), I850 (≠ A514), T882 (= T542), A883 (= A543), F887 (≠ V548), G888 (= G549), Q891 (≠ R552)
- binding calcium ion: E713 (≠ A373), H714 (= H374), Y716 (≠ T376), T809 (≠ D465), G810 (≠ M466), G840 (≠ P504), T843 (≠ K507), E844 (≠ N508), S847 (≠ D511), S880 (vs. gap), N881 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L717 (≠ M377)
- binding uric acid: E775 (≠ R432), R853 (≠ V517), F887 (≠ V548)
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
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
24% identity, 47% coverage: 216:565/750 of query aligns to 527:904/1295 of 6a7xA
- active site: Q740 (= Q398), E775 (≠ R432), R853 (≠ V517), H857 (vs. gap), R885 (= R546)
- binding bicarbonate ion: R812 (= R468), H813 (≠ P469), I850 (≠ A514), A883 (= A543), F884 (= F544), F887 (≠ V548), G888 (= G549), Q891 (≠ R552)
- binding uric acid: E775 (≠ R432), R853 (≠ V517), F887 (≠ V548)
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
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
24% identity, 47% coverage: 216:565/750 of query aligns to 525:902/1286 of 4yswA
- active site: Q738 (= Q398), E773 (≠ R432), R851 (≠ V517), H855 (vs. gap), R883 (= R546)
- binding bicarbonate ion: R810 (= R468), H811 (≠ P469), I848 (≠ A514), T880 (= T542), A881 (= A543), F882 (= F544), F885 (≠ V548), G886 (= G549), Q889 (≠ R552)
- binding calcium ion: G838 (≠ P504), T841 (≠ K507), E842 (≠ N508), S845 (≠ D511), S878 (vs. gap), N879 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M377)
- binding uric acid: E773 (≠ R432), R851 (≠ V517), F885 (≠ V548)
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
P22985 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 47% coverage: 216:565/750 of query aligns to 554:931/1331 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.
8emtB Cryo-em analysis of the human aldehyde oxidase from liver (see paper)
22% identity, 48% coverage: 220:576/750 of query aligns to 483:836/1221 of 8emtB
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 210, 211, 213, 214, 216, 217, 218, 291, 292, 300, 304, 305, 307, 314
- binding fe2/s2 (inorganic) cluster: 38, 39, 40, 42, 44, 45, 47, 69, 109, 112, 144, 146
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
21% identity, 46% coverage: 230:576/750 of query aligns to 545:905/1290 of 4uhxA
Sites not aligning to the query:
- active site: 1223, 1224
- binding flavin-adenine dinucleotide: 43, 44, 229, 230, 231, 232, 233, 234, 235, 236, 237, 310, 311, 319, 320, 323, 324, 326, 329, 332, 333, 377, 404
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 111, 112, 114, 146, 148
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: 540, 542, 543, 1014, 1015, 1018, 1019, 1020, 1079
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: 540, 542, 543, 1014, 1015, 1018, 1019, 1020
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
34% identity, 15% coverage: 632:743/750 of query aligns to 577:695/701 of 4zohA
Sites not aligning to the query:
- active site: 186, 219, 298, 300, 304, 332
- binding pterin cytosine dinucleotide: 213, 214, 215, 332, 442, 443, 444, 446, 482, 484, 486, 487
2ckjA Human milk xanthine oxidoreductase
23% identity, 47% coverage: 229:582/750 of query aligns to 516:892/1264 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
>BPHYT_RS24635 FitnessBrowser__BFirm:BPHYT_RS24635
MSQGLLDSQNGTQASKAGARAAGGLSRRTFLKFGVTVGAAAGGGLLLGFSMPAASQDQKA
GKSVIGGDGVEAPQSGVFAPNAFIQIDTAGKVTLVIPKVEMGQGVYTSIPMLIAEELEVP
LDSITIDHAPPNEKLFMDPLLGGQLTGGSTSIRYAWEPMRKAGATARTVLISAAAQQWQV
DPASCHAQGGQVIHEASKRSVSYGELVTAAAGLPAPQNVKLKDPKDFKLIGTAVKRLDSP
EKVDGTAMFGLDVRVPDMVYAAIANCPVFGGTLASVDDTNAKKIPGVRQVIKIDNAVAVI
GDHTWAAKRGVQALVIKWNEGAGANLSMKQIVDDLANASQRDGAVARKDGDVGNAFSNAK
TRVDAVYQQPFLAHATMEPINCTVHVRPDGCDVWLGSQVPTRVVDAAAAVTGLPADKIVV
HNHLIGGGFGRRLEFDMVTQAVKVAKQVSTPVKVVWTREEDIQHDMYRPYYYDKISAGLD
ANGKPVAWQHRIVGSSVMARFAPPAFKNGIDPDAVEVAADLPYDLPNQLIDYVRQEPHTV
PTAFWRGVGPTRGTFVVESFIDELAAQAKVDPVKYRQDLLGKTPRALSVLNVATQAANWG
SAVPKGQGRGVSVMHAFGSFFAIVVDVAVEQGEVAVKRVVCAVDCGMVVNPNTIEAQVQG
GIIFGITAALYGEITIKDGRVEQNNFTDYRMLRIDQTPPIEVHIVKSSEAPGGIGEPGTA
ALAPALTNAIYAATGKRLRQLPVGSQLQTV
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