SitesBLAST
Comparing WP_057507174.1 NCBI__GCF_001431535.1:WP_057507174.1 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)
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
39% identity, 97% coverage: 23:758/759 of query aligns to 8:748/748 of 5y6qC
- active site: Q204 (= Q229), P239 (≠ L264), A310 (≠ V334), V316 (≠ W340), R344 (= R368), E715 (= E725), L716 (≠ I726)
- binding pterin cytosine dinucleotide: G233 (= G258), G234 (≠ A259), F235 (= F260), I461 (= I485), G462 (= G486), T463 (= T487), G464 (= G488), I468 (≠ V492), G500 (= G524), S502 (= S526), Q503 (≠ S527), L504 (≠ H528), A505 (≠ V529), R638 (= R648), Y640 (≠ L650), N641 (= N651), Q648 (= Q658), K711 (= K721), V713 (= V723), G714 (= G724), E715 (= E725)
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 96% coverage: 28:758/759 of query aligns to 24:725/732 of P77489
- GF 241:242 (≠ AF 259:260) binding
- R440 (≠ W457) mutation R->H,K: Decrease in catalytic efficiency.
- IGT 468:470 (= IGT 485:487) binding
- GA 511:512 (≠ HV 528:529) binding
- 615:621 (vs. 648:654, 86% identical) binding
- Q625 (= Q658) binding
- KGVG 688:691 (= KGVG 721:724) binding
- E692 (= E725) mutation to Q: Loss of activity.
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
39% identity, 96% coverage: 28:758/759 of query aligns to 24:725/731 of 5g5gC
- active site: Q211 (= Q229), L246 (= L264), P316 (≠ V334), Q322 (≠ W340), R350 (= R368), E692 (= E725), L693 (≠ I726)
- binding pterin cytosine dinucleotide: G240 (= G258), G241 (≠ A259), F242 (= F260), R350 (= R368), I468 (= I485), G469 (= G486), T470 (= T487), G507 (= G524), Q509 (≠ S526), G511 (≠ H528), A512 (≠ V529), L617 (= L650), N618 (= N651), T621 (= T654), Q625 (= Q658), K688 (= K721), V690 (= V723), G691 (= G724), E692 (= E725)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
28% identity, 99% coverage: 5:757/759 of query aligns to 3:758/769 of O33819
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
28% identity, 97% coverage: 23:757/759 of query aligns to 4:750/761 of 1rm6A
- active site: Q206 (= Q229), T241 (≠ L264), Y318 (≠ W340), L322 (= L344), R350 (= R368), E718 (= E725), G719 (≠ I726)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G258), G236 (≠ A259), F237 (= F260), G238 (= G261), R350 (= R368), I473 (= I485), G474 (= G486), Q475 (≠ T487), G476 (= G488), Y513 (vs. gap), S514 (= S526), S515 (= S527), V517 (= V529), T518 (≠ S530), L646 (= L650), N647 (= N651), V651 (≠ A655), Q654 (= Q658), K714 (= K721), E715 (≠ G722), A716 (≠ V723), S717 (≠ G724), E718 (= E725)
4usaA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with trans-cinnamaldehyde (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of 4usaA
- active site: I390 (≠ Q229), F425 (≠ L264), R501 (vs. gap), F505 (≠ W340), R533 (= R368), E869 (= E725), L870 (≠ I726)
- binding bicarbonate ion: R460 (= R299), A531 (≠ D366), F532 (≠ M367), Y535 (≠ P370), Q539 (≠ H374)
- binding hydrocinnamic acid: I255 (≠ F97), F425 (≠ L264), F494 (≠ Y333), L497 (≠ V336), Y535 (≠ P370), L626 (vs. gap)
- binding magnesium ion: E899 (≠ D755)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ A259), F421 (= F260), G422 (= G261), R533 (= R368), W650 (≠ A482), H653 (≠ I485), G654 (= G486), Q655 (≠ T487), G656 (= G488), S695 (≠ E523), G696 (= G524), G697 (= G525), Q700 (≠ H528), Q701 (≠ V529), C799 (≠ L650), N800 (= N651), T804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding magnesium ion: 903
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
4us9A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with 3- phenylpropionaldehyde (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of 4us9A
- active site: I390 (≠ Q229), F425 (≠ L264), R501 (vs. gap), F505 (≠ W340), R533 (= R368), E869 (= E725), L870 (≠ I726)
- binding 3-phenylpropanal: I255 (≠ F97), F257 (≠ K99), P258 (≠ D100), H752 (≠ S597)
- binding bicarbonate ion: R460 (= R299), L498 (≠ V337), A531 (≠ D366), F532 (≠ M367), Y535 (≠ P370), Q539 (≠ H374), R890 (= R746), Y892 (≠ R748)
- binding magnesium ion: E899 (≠ D755)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ A259), F421 (= F260), G422 (= G261), R533 (= R368), W650 (≠ A482), H653 (≠ I485), G654 (= G486), Q655 (≠ T487), G656 (= G488), S695 (≠ E523), G696 (= G524), G697 (= G525), Q700 (≠ H528), Q701 (≠ V529), C799 (≠ L650), N800 (= N651), T804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding magnesium ion: 903
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
4us8A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with benzaldehyde (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of 4us8A
- active site: I390 (≠ Q229), F425 (≠ L264), R501 (vs. gap), F505 (≠ W340), R533 (= R368), E869 (= E725), L870 (≠ I726)
- binding bicarbonate ion: R460 (= R299), L498 (≠ V337), A531 (≠ D366), F532 (≠ M367), Y535 (≠ P370), Q539 (≠ H374)
- binding benzaldehyde: I255 (≠ F97), I255 (≠ F97), L394 (≠ N233), F425 (≠ L264), F425 (≠ L264), F425 (≠ L264), F425 (≠ L264), L497 (≠ V336), L497 (≠ V336), R501 (vs. gap), A531 (≠ D366), Y535 (≠ P370), Y535 (≠ P370), L626 (vs. gap), L626 (vs. gap), L626 (vs. gap), P694 (≠ I522), G696 (= G524), G697 (= G525)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ A259), F421 (= F260), G422 (= G261), R533 (= R368), H653 (≠ I485), G654 (= G486), Q655 (≠ T487), G656 (= G488), S695 (≠ E523), G696 (= G524), G697 (= G525), Q700 (≠ H528), Q701 (≠ V529), C799 (≠ L650), N800 (= N651), T804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
4c7yA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with sodium dithionite and sodium sulfide (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of 4c7yA
- active site: I390 (≠ Q229), F425 (≠ L264), R501 (vs. gap), F505 (≠ W340), R533 (= R368), E869 (= E725), L870 (≠ I726)
- binding bicarbonate ion: R460 (= R299), L498 (≠ V337), A531 (≠ D366), Y535 (≠ P370), Q539 (≠ H374)
- binding magnesium ion: E899 (≠ D755)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ A259), F421 (= F260), G422 (= G261), R533 (= R368), W650 (≠ A482), H653 (≠ I485), G654 (= G486), Q655 (≠ T487), G656 (= G488), S695 (≠ E523), G696 (= G524), Q700 (≠ H528), Q701 (≠ V529), C799 (≠ L650), N800 (= N651), T804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
- binding hydrogen peroxide: G696 (= G524), G697 (= G525), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding magnesium ion: 903
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
3fc4A Ethylene glycol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of 3fc4A
- active site: I390 (≠ Q229), F425 (≠ L264), R501 (vs. gap), F505 (≠ W340), R533 (= R368), E869 (= E725), L870 (≠ I726)
- binding 1,2-ethanediol: Y535 (≠ P370), Y622 (≠ W457), G696 (= G524), G697 (= G525), E869 (= E725)
- binding magnesium ion: E899 (≠ D755)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G419 (= G258), T420 (≠ A259), F421 (= F260), G422 (= G261), R533 (= R368), W650 (≠ A482), H653 (≠ I485), G654 (= G486), Q655 (≠ T487), G656 (= G488), S695 (≠ E523), G696 (= G524), Q700 (≠ H528), Q701 (≠ V529), C799 (≠ L650), N800 (= N651), T804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding magnesium ion: 903
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
3fahA Glycerol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of 3fahA
- active site: I390 (≠ Q229), F425 (≠ L264), R501 (vs. gap), F505 (≠ W340), R533 (= R368), E869 (= E725), L870 (≠ I726)
- binding glycerol: P416 (≠ A254), Y535 (≠ P370), Y622 (≠ W457), W683 (≠ L512), G696 (= G524), G697 (= G525), E869 (= E725), K884 (≠ H740), V889 (≠ K745), R890 (= R746), Y892 (≠ R748)
- binding magnesium ion: E899 (≠ D755)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G419 (= G258), T420 (≠ A259), F421 (= F260), G422 (= G261), R533 (= R368), W650 (≠ A482), H653 (≠ I485), G654 (= G486), Q655 (≠ T487), G656 (= G488), S695 (≠ E523), G696 (= G524), Q700 (≠ H528), Q701 (≠ V529), C799 (≠ L650), N800 (= N651), T804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding magnesium ion: 903
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
1sijA Crystal structure of the aldehyde dehydrogenase (a.K.A. Aor or mop) of desulfovibrio gigas covalently bound to [aso3]- (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of 1sijA
- active site: I390 (≠ Q229), F425 (≠ L264), R501 (vs. gap), F505 (≠ W340), R533 (= R368), E869 (= E725), L870 (≠ I726)
- binding arsenite: Y535 (≠ P370), G696 (= G524), G697 (= G525), E869 (= E725)
- binding magnesium ion: E899 (≠ D755)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ A259), F421 (= F260), G422 (= G261), R533 (= R368), H653 (≠ I485), G654 (= G486), Q655 (≠ T487), G656 (= G488), S695 (≠ E523), G696 (= G524), S698 (= S526), Q700 (≠ H528), Q701 (≠ V529), C799 (≠ L650), N800 (= N651), T804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 40, 41, 43, 45, 46, 48, 58, 60, 99, 100, 101, 103, 137, 139
- binding magnesium ion: 903
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
Q46509 Aldehyde oxidoreductase; Molybdenum iron sulfur protein; EC 1.2.99.7 from Megalodesulfovibrio gigas (Desulfovibrio gigas) (see paper)
28% identity, 97% coverage: 23:758/759 of query aligns to 177:902/907 of Q46509
Sites not aligning to the query:
- 40 binding
- 45 binding
- 48 binding
- 60 binding
- 100 binding
- 103 binding
- 137 binding
- 139 binding
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
26% identity, 89% coverage: 76:752/759 of query aligns to 28:695/701 of 4zohA
- active site: Q186 (= Q229), I219 (≠ L264), V298 (≠ L344), S300 (≠ A346), M304 (≠ V350), R332 (= R368), E668 (= E725), A669 (≠ I726)
- binding pterin cytosine dinucleotide: G213 (= G258), A214 (= A259), F215 (= F260), R332 (= R368), H442 (≠ I485), G443 (= G486), Q444 (≠ T487), D446 (≠ T489), W482 (≠ G524), S484 (= S526), T486 (≠ H528), V487 (= V529), I594 (≠ L650), N595 (= N651), L598 (≠ T654), Q602 (= Q658), K664 (= K721), G665 (= G722), I666 (≠ V723), G667 (= G724), E668 (= E725)
7dqxD Crystal structure of xanthine dehydrogenase family protein
24% identity, 92% coverage: 28:725/759 of query aligns to 12:728/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G258), S248 (≠ A259), F249 (= F260), R363 (= R368), V491 (≠ I485), G492 (= G486), Q493 (≠ T487), G494 (= G488), V498 (= V492), S530 (≠ H528), W531 (≠ V529), S532 (= S530), S533 (≠ T531), R534 (≠ V532), S535 (≠ G533), T536 (≠ S534), T658 (= T654), T659 (≠ A655), Q662 (= Q658), G725 (= G722), L726 (≠ V723), G727 (= G724), E728 (= E725)
1dgjA Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774 (see paper)
26% identity, 97% coverage: 23:758/759 of query aligns to 177:902/906 of 1dgjA
- active site: V391 (≠ Q229), F427 (≠ L264), R503 (≠ V337), Y507 (≠ W340), R535 (= R368), E869 (= E725), M870 (≠ I726)
- binding molybdenum (iv)oxide: G424 (= G261), R535 (= R368), G698 (= G524), E869 (= E725)
- binding pterin cytosine dinucleotide: F423 (= F260), G424 (= G261), R535 (= R368), W652 (≠ A482), H655 (≠ I485), G656 (= G486), Q657 (≠ T487), G658 (= G488), A697 (≠ E523), G698 (= G524), S700 (= S526), S702 (≠ H528), Q703 (≠ V529), C799 (≠ L650), N800 (= N651), V803 (≠ T654), V804 (≠ A655), Q807 (= Q658), S865 (≠ K721), G866 (= G722), V867 (= V723), G868 (= G724), E869 (= E725)
Sites not aligning to the query:
- binding fe2/s2 (inorganic) cluster: 38, 39, 40, 41, 43, 44, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding pterin cytosine dinucleotide: 99, 139
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
25% identity, 97% coverage: 23:758/759 of query aligns to 15:779/786 of 1t3qB
- active site: Q224 (= Q229), A259 (≠ L264), E336 (≠ A346), V343 (vs. gap), R371 (= R368), E743 (= E725), S744 (≠ I726)
- binding pterin cytosine dinucleotide: G254 (≠ A259), F255 (= F260), R371 (= R368), S506 (≠ I485), G507 (= G486), Q508 (≠ T487), H510 (≠ T489), T513 (≠ V492), Y545 (≠ G525), S547 (= S527), G549 (≠ V529), A550 (≠ S530), C666 (≠ A646), I670 (≠ L650), I674 (≠ T654), V675 (≠ A655), Q678 (= Q658), K739 (= K721), G740 (= G722), M741 (≠ V723), G742 (= G724)
3hrdB Crystal structure of nicotinate dehydrogenase (see paper)
32% identity, 42% coverage: 439:759/759 of query aligns to 4:323/330 of 3hrdB
- active site: E289 (= E725), P290 (≠ I726)
- binding pterin cytosine dinucleotide: I45 (= I485), G46 (= G486), Q47 (≠ T487), G48 (= G488), S49 (≠ T489), S85 (≠ H528), S87 (= S530), Q89 (vs. gap), T90 (vs. gap), I215 (≠ L650), N216 (= N651), M219 (≠ T654), V220 (≠ A655), Q223 (= Q658), K285 (= K721), G286 (= G722), V287 (= V723), G288 (= G724), E289 (= E725)
- binding nicotinic acid: N17 (≠ A453), T18 (= T454)
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)
32% identity, 42% coverage: 439:759/759 of query aligns to 4:323/330 of Q0QLF1
2w54B Crystal structure of xanthine dehydrogenase from rhodobacter capsulatus in complex with bound inhibitor pterin-6-aldehyde (see paper)
26% identity, 97% coverage: 23:759/759 of query aligns to 3:751/760 of 2w54B
- active site: Q196 (= Q229), E231 (vs. gap), R309 (≠ N349), H313 (vs. gap), R341 (= R368), G712 (= G724), E713 (= E725)
- binding 6-hydroxymethylpterin: E231 (vs. gap), P305 (vs. gap), R309 (≠ N349), F343 (≠ P370), F442 (= F463), T443 (≠ A464), L444 (≠ R465), A512 (≠ G525), E713 (= E725)
- binding {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-kappaS)-3,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2-) phosphate}(hydroxy)oxo(thioxo)molybdenum: G226 (≠ A259), F227 (= F260), G228 (vs. gap), F340 (≠ M367), R341 (= R368), M471 (≠ I485), G472 (= G486), Q473 (≠ T487), A511 (≠ G524), S513 (= S526), G515 (≠ H528), Q646 (= Q658), E713 (= E725)
Query Sequence
>WP_057507174.1 NCBI__GCF_001431535.1:WP_057507174.1
MSAYPKQPQVPVAEPGTGHVPTGTGTPRIDGRAKVTGQARYAAEWPATDLVYGVVVNSSI
AKGRILGFDLDAAQAVPGVLKVLTHLNRPHMRGAGIFYKDMTAPAGSPFRPLYDAQVRYS
GQPVALVLAETFEAARHAAGLVEVRYKTEAHETNLVASVERAREPRKMKAGFSAPPKDKG
EPNQAFAQAAHRISADFYSGVEHHNPMELFASTVIRDDDGHLTIHDKTQGSQNSRWYVSH
VFGLPKRKVTVRNAYVGGAFGSGLRPQYQLPLAVMGALALERSVRVVLTRQQMFTFGHRP
ETVQRVKLAADADGTLRSIWHEAVAETSRIEDYVEVVVNWSGQLYACDNVHVGYKVVDLD
QYTPIDMRAPGASHGMHALEVAMDELANEVGIDPLALRLKNYAETNPADGKPFSTKALRE
CYRRGAERFGWADRAPLPRARREGNEWVGWGMATGQWDAMQMFARAHAELHADGRLVVSS
AATDIGTGTYTVMSMIAAEALGLPLEQVTFQLGDSTLPVAPIEGGSSHVSTVGSAVDGAC
AKLRRQLLALAAGTQYSAFNRAGLDDVVFANGTLALRDDPASAIALTTLLADAGKASIEA
KYLLLPNVLKQRRYTRATHSAVFVEVRVDEELGTVRVMRVVSAIAAGRILNPTTARSQII
GGVVWGIGAALHEHTESDHRFGRFMNHDLAQYHVSVNADIHDVDVLFVEEDDRVVSSLGA
KGVGEIGLVGVSAAICNAIHHATGKRIRSTPITPDKVMA
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