SitesBLAST
Comparing AZOBR_RS29690 FitnessBrowser__azobra:AZOBR_RS29690 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)
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
37% identity, 97% coverage: 15:782/789 of query aligns to 14:782/786 of 1t3qB
- active site: Q224 (= Q222), A259 (≠ G257), E336 (= E334), V343 (≠ I341), R371 (= R369), E743 (= E743), S744 (≠ G744)
- binding pterin cytosine dinucleotide: G254 (= G252), F255 (= F253), R371 (= R369), S506 (≠ H505), G507 (= G506), Q508 (= Q507), H510 (≠ M509), T513 (= T512), Y545 (≠ W545), S547 (= S547), G549 (≠ S549), A550 (≠ M550), C666 (≠ A666), I670 (≠ V670), I674 (≠ V674), V675 (= V675), Q678 (= Q678), K739 (= K739), G740 (= G740), M741 (≠ I741), G742 (= G742)
1ffvB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava (see paper)
32% identity, 97% coverage: 11:774/789 of query aligns to 8:782/797 of 1ffvB
- active site: Q231 (= Q222), V266 (≠ G257), P343 (vs. gap), I349 (= I341), R378 (= R369), C379 (≠ G370), E751 (= E743), S752 (≠ G744)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G251), G261 (= G252), F262 (= F253), G263 (= G254), A376 (≠ P367), R378 (= R369), C379 (≠ G370), Q516 (≠ H505), G517 (= G506), Q518 (= Q507), H520 (≠ M509), T523 (= T512), Y556 (≠ W545), G557 (= G546), S558 (= S547), S560 (= S549), T561 (≠ M550), C674 (≠ A666), I678 (≠ V670), I683 (≠ V675), Q686 (= Q678), K747 (= K739), G748 (= G740), V749 (≠ I741), A750 (≠ G742), E751 (= E743)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
32% identity, 97% coverage: 11:774/789 of query aligns to 8:782/797 of 1ffuB
- active site: Q231 (= Q222), V266 (≠ G257), P343 (vs. gap), I349 (= I341), R378 (= R369), C379 (≠ G370), E751 (= E743), S752 (≠ G744)
- binding cytidine-5'-diphosphate: Q518 (= Q507), H520 (≠ M509), T523 (= T512), S558 (= S547), S560 (= S549), T561 (≠ M550), C674 (≠ A666), T676 (= T668), I678 (≠ V670), I683 (≠ V675), K747 (= K739), G748 (= G740), V749 (≠ I741), A750 (≠ G742)
P19913 Carbon monoxide dehydrogenase large chain; CO dehydrogenase subunit L; CO-DH L; EC 1.2.5.3 from Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava) (see paper)
32% identity, 97% coverage: 11:774/789 of query aligns to 14:788/803 of P19913
- R384 (= R369) modified: 4-hydroxyarginine
7dqxD Crystal structure of xanthine dehydrogenase family protein
32% identity, 98% coverage: 15:784/789 of query aligns to 6:768/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G251), S248 (≠ G252), F249 (= F253), R363 (= R369), V491 (≠ H505), G492 (= G506), Q493 (= Q507), G494 (≠ S508), V498 (≠ T512), S530 (≠ T544), W531 (= W545), S532 (≠ G546), S533 (= S547), R534 (= R548), S535 (= S549), T536 (≠ M550), T658 (≠ V674), T659 (≠ V675), Q662 (= Q678), G725 (= G740), L726 (≠ I741), G727 (= G742), E728 (= E743)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
32% identity, 95% coverage: 15:762/789 of query aligns to 3:687/701 of 4zohA
- active site: Q186 (= Q222), I219 (≠ G257), V298 (= V338), S300 (= S340), M304 (≠ I341), R332 (= R369), E668 (= E743), A669 (≠ G744)
- binding pterin cytosine dinucleotide: G213 (= G251), A214 (≠ G252), F215 (= F253), R332 (= R369), H442 (= H505), G443 (= G506), Q444 (= Q507), D446 (≠ M509), W482 (= W545), S484 (= S547), T486 (≠ S549), V487 (≠ M550), I594 (≠ V670), N595 (= N671), L598 (≠ V674), Q602 (= Q678), K664 (= K739), G665 (= G740), I666 (= I741), G667 (= G742), E668 (= E743)
P19919 Carbon monoxide dehydrogenase large chain; CO dehydrogenase subunit L; CO-DH L; EC 1.2.5.3 from Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) (Oligotropha carboxidovorans) (see 2 papers)
31% identity, 95% coverage: 13:765/789 of query aligns to 19:785/809 of P19919
- C388 (≠ G370) binding
- E763 (= E743) binding
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
31% identity, 95% coverage: 13:765/789 of query aligns to 14:780/804 of 1zxiB
- active site: Q235 (= Q222), V270 (≠ G257), P347 (vs. gap), I353 (= I341), R382 (= R369), C383 (≠ G370), E758 (= E743), S759 (≠ G744)
- binding copper (ii) ion: C383 (≠ G370), S384 (≠ V371), E758 (= E743)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F253), G267 (= G254), A380 (≠ P367), Y381 (= Y368), R382 (= R369), C383 (≠ G370), Y563 (≠ W545), G564 (= G546), E758 (= E743)
- binding pterin cytosine dinucleotide: G265 (= G252), F266 (= F253), R382 (= R369), Q523 (≠ H505), G524 (= G506), Q525 (= Q507), H527 (≠ M509), T530 (= T512), T562 (= T544), Y563 (≠ W545), S565 (= S547), S567 (= S549), T568 (≠ M550), C681 (≠ A666), I685 (≠ V670), I689 (≠ V674), I690 (≠ V675), Q693 (= Q678), K754 (= K739), G755 (= G740), V756 (≠ I741), E758 (= E743)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
31% identity, 95% coverage: 13:765/789 of query aligns to 14:780/804 of 1n62B
- active site: Q235 (= Q222), V270 (≠ G257), P347 (vs. gap), I353 (= I341), R382 (= R369), C383 (≠ G370), E758 (= E743), S759 (≠ G744)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G254), V379 (= V366), A380 (≠ P367), R382 (= R369), C383 (≠ G370), F385 (≠ A372), Y563 (≠ W545), G564 (= G546), E758 (= E743)
- binding pterin cytosine dinucleotide: G265 (= G252), F266 (= F253), R382 (= R369), Q523 (≠ H505), G524 (= G506), Q525 (= Q507), H527 (≠ M509), T530 (= T512), T562 (= T544), Y563 (≠ W545), G564 (= G546), S565 (= S547), S567 (= S549), T568 (≠ M550), C681 (≠ A666), I685 (≠ V670), I689 (≠ V674), I690 (≠ V675), Q693 (= Q678), K754 (= K739), G755 (= G740), V756 (≠ I741), G757 (= G742), E758 (= E743)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
31% identity, 95% coverage: 13:765/789 of query aligns to 14:780/804 of 1n5wB
- active site: Q235 (= Q222), V270 (≠ G257), P347 (vs. gap), I353 (= I341), R382 (= R369), C383 (≠ G370), E758 (= E743), S759 (≠ G744)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G254), A380 (≠ P367), R382 (= R369), C383 (≠ G370), Y563 (≠ W545), G564 (= G546), E758 (= E743)
- binding pterin cytosine dinucleotide: G265 (= G252), F266 (= F253), R382 (= R369), Q523 (≠ H505), G524 (= G506), Q525 (= Q507), H527 (≠ M509), T530 (= T512), T562 (= T544), Y563 (≠ W545), S565 (= S547), S567 (= S549), T568 (≠ M550), C681 (≠ A666), I685 (≠ V670), I689 (≠ V674), I690 (≠ V675), Q693 (= Q678), K754 (= K739), G755 (= G740), V756 (≠ I741), E758 (= E743)
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
31% identity, 95% coverage: 13:765/789 of query aligns to 15:781/805 of 1n63B
- active site: Q236 (= Q222), V271 (≠ G257), P348 (vs. gap), I354 (= I341), R383 (= R369), C384 (≠ G370), E759 (= E743), S760 (≠ G744)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G254), A381 (≠ P367), R383 (= R369), C384 (≠ G370), Y564 (≠ W545), G565 (= G546), E759 (= E743)
- binding pterin cytosine dinucleotide: G266 (= G252), F267 (= F253), R383 (= R369), Q524 (≠ H505), G525 (= G506), Q526 (= Q507), H528 (≠ M509), T531 (= T512), T563 (= T544), Y564 (≠ W545), S566 (= S547), S568 (= S549), T569 (≠ M550), C682 (≠ A666), I686 (≠ V670), I690 (≠ V674), I691 (≠ V675), Q694 (= Q678), K755 (= K739), G756 (= G740), V757 (≠ I741), E759 (= E743)
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
31% identity, 95% coverage: 13:765/789 of query aligns to 13:779/803 of 1n60B
- active site: Q234 (= Q222), V269 (≠ G257), P346 (vs. gap), I352 (= I341), R381 (= R369), C382 (≠ G370), E757 (= E743), S758 (≠ G744)
- binding pterin cytosine dinucleotide: G264 (= G252), F265 (= F253), R381 (= R369), Q522 (≠ H505), G523 (= G506), Q524 (= Q507), H526 (≠ M509), T529 (= T512), T561 (= T544), Y562 (≠ W545), G563 (= G546), S564 (= S547), S566 (= S549), T567 (≠ M550), C680 (≠ A666), I684 (≠ V670), I688 (≠ V674), I689 (≠ V675), Q692 (= Q678), K753 (= K739), G754 (= G740), V755 (≠ I741), E757 (= E743)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F253), G266 (= G254), Y562 (≠ W545), G563 (= G546), E757 (= E743)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
29% identity, 98% coverage: 15:789/789 of query aligns to 3:761/761 of 1rm6A
- active site: Q206 (= Q222), T241 (≠ G257), Y318 (≠ Q337), L322 (≠ I341), R350 (= R369), E718 (= E743), G719 (= G744)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G251), G236 (= G252), F237 (= F253), G238 (= G254), R350 (= R369), I473 (≠ H505), G474 (= G506), Q475 (= Q507), G476 (≠ S508), Y513 (≠ W545), S514 (≠ G546), S515 (= S547), V517 (≠ S549), T518 (≠ M550), L646 (≠ V670), N647 (= N671), V651 (= V675), Q654 (= Q678), K714 (= K739), E715 (≠ G740), A716 (≠ I741), S717 (≠ G742), E718 (= E743)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
29% identity, 98% coverage: 15:789/789 of query aligns to 11:769/769 of O33819
1dgjA Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774 (see paper)
28% identity, 93% coverage: 46:782/789 of query aligns to 210:905/906 of 1dgjA
- active site: V391 (≠ Q222), F427 (≠ G257), R503 (≠ E334), Y507 (≠ V338), R535 (= R369), E869 (= E743), M870 (≠ G744)
- binding molybdenum (iv)oxide: G424 (= G254), R535 (= R369), G698 (≠ W545), E869 (= E743)
- binding pterin cytosine dinucleotide: F423 (= F253), G424 (= G254), R535 (= R369), W652 (≠ V502), H655 (= H505), G656 (= G506), Q657 (= Q507), G658 (≠ S508), A697 (≠ T544), G698 (≠ W545), S700 (= S547), S702 (= S549), Q703 (≠ M550), C799 (≠ V670), N800 (= N671), V803 (= V674), V804 (= V675), Q807 (= Q678), S865 (≠ K739), G866 (= G740), V867 (≠ I741), G868 (= G742), E869 (= E743)
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
4usaA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with trans-cinnamaldehyde (see paper)
27% identity, 94% coverage: 42:782/789 of query aligns to 206:905/907 of 4usaA
- active site: I390 (≠ T221), F425 (≠ G257), R501 (≠ E334), F505 (≠ I341), R533 (= R369), E869 (= E743), L870 (≠ G744)
- binding bicarbonate ion: R460 (≠ A293), A531 (≠ P367), F532 (≠ Y368), Y535 (≠ V371), Q539 (≠ G375)
- binding hydrocinnamic acid: I255 (≠ P92), F425 (≠ G257), F494 (≠ Y327), L497 (≠ S330), Y535 (≠ V371), L626 (≠ I477)
- binding magnesium ion: E899 (= E776), E903 (≠ T780)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G252), F421 (= F253), G422 (= G254), R533 (= R369), W650 (≠ V502), H653 (= H505), G654 (= G506), Q655 (= Q507), G656 (≠ S508), S695 (≠ T544), G696 (≠ W545), G697 (= G546), Q700 (≠ S549), Q701 (≠ M550), C799 (≠ V670), N800 (= N671), T804 (≠ V675), Q807 (= Q678), S865 (≠ K739), G866 (= G740), V867 (≠ I741), G868 (= G742), E869 (= E743)
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
4us9A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with 3- phenylpropionaldehyde (see paper)
27% identity, 94% coverage: 42:782/789 of query aligns to 206:905/907 of 4us9A
- active site: I390 (≠ T221), F425 (≠ G257), R501 (≠ E334), F505 (≠ I341), R533 (= R369), E869 (= E743), L870 (≠ G744)
- binding 3-phenylpropanal: I255 (≠ P92), F257 (= F94), P258 (≠ K95), H752 (≠ E623)
- binding bicarbonate ion: R460 (≠ A293), L498 (≠ A331), A531 (≠ P367), F532 (≠ Y368), Y535 (≠ V371), Q539 (≠ G375), R890 (≠ I767), Y892 (≠ T769)
- binding magnesium ion: E899 (= E776), E903 (≠ T780)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G252), F421 (= F253), G422 (= G254), R533 (= R369), W650 (≠ V502), H653 (= H505), G654 (= G506), Q655 (= Q507), G656 (≠ S508), S695 (≠ T544), G696 (≠ W545), G697 (= G546), Q700 (≠ S549), Q701 (≠ M550), C799 (≠ V670), N800 (= N671), T804 (≠ V675), Q807 (= Q678), S865 (≠ K739), G866 (= G740), V867 (≠ I741), G868 (= G742), E869 (= E743)
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
4us8A Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with benzaldehyde (see paper)
27% identity, 94% coverage: 42:782/789 of query aligns to 206:905/907 of 4us8A
- active site: I390 (≠ T221), F425 (≠ G257), R501 (≠ E334), F505 (≠ I341), R533 (= R369), E869 (= E743), L870 (≠ G744)
- binding bicarbonate ion: R460 (≠ A293), L498 (≠ A331), A531 (≠ P367), F532 (≠ Y368), Y535 (≠ V371), Q539 (≠ G375)
- binding benzaldehyde: I255 (≠ P92), I255 (≠ P92), L394 (≠ I226), F425 (≠ G257), F425 (≠ G257), F425 (≠ G257), F425 (≠ G257), L497 (≠ S330), L497 (≠ S330), R501 (≠ E334), A531 (≠ P367), Y535 (≠ V371), Y535 (≠ V371), L626 (≠ I477), L626 (≠ I477), L626 (≠ I477), P694 (≠ G543), G696 (≠ W545), G697 (= G546)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G252), F421 (= F253), G422 (= G254), R533 (= R369), H653 (= H505), G654 (= G506), Q655 (= Q507), G656 (≠ S508), S695 (≠ T544), G696 (≠ W545), G697 (= G546), Q700 (≠ S549), Q701 (≠ M550), C799 (≠ V670), N800 (= N671), T804 (≠ V675), Q807 (= Q678), S865 (≠ K739), G866 (= G740), V867 (≠ I741), G868 (= G742), E869 (= E743)
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)
27% identity, 94% coverage: 42:782/789 of query aligns to 206:905/907 of 4c7yA
- active site: I390 (≠ T221), F425 (≠ G257), R501 (≠ E334), F505 (≠ I341), R533 (= R369), E869 (= E743), L870 (≠ G744)
- binding bicarbonate ion: R460 (≠ A293), L498 (≠ A331), A531 (≠ P367), Y535 (≠ V371), Q539 (≠ G375)
- binding magnesium ion: E899 (= E776), E903 (≠ T780)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G252), F421 (= F253), G422 (= G254), R533 (= R369), W650 (≠ V502), H653 (= H505), G654 (= G506), Q655 (= Q507), G656 (≠ S508), S695 (≠ T544), G696 (≠ W545), Q700 (≠ S549), Q701 (≠ M550), C799 (≠ V670), N800 (= N671), T804 (≠ V675), Q807 (= Q678), S865 (≠ K739), G866 (= G740), V867 (≠ I741), G868 (= G742), E869 (= E743)
- binding hydrogen peroxide: G696 (≠ W545), G697 (= G546), E869 (= E743)
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 (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 99, 139
3fc4A Ethylene glycol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas (see paper)
27% identity, 94% coverage: 42:782/789 of query aligns to 206:905/907 of 3fc4A
- active site: I390 (≠ T221), F425 (≠ G257), R501 (≠ E334), F505 (≠ I341), R533 (= R369), E869 (= E743), L870 (≠ G744)
- binding 1,2-ethanediol: Y535 (≠ V371), Y622 (= Y461), G696 (≠ W545), G697 (= G546), E869 (= E743)
- binding magnesium ion: E899 (= E776), E903 (≠ T780)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G419 (= G251), T420 (≠ G252), F421 (= F253), G422 (= G254), R533 (= R369), W650 (≠ V502), H653 (= H505), G654 (= G506), Q655 (= Q507), G656 (≠ S508), S695 (≠ T544), G696 (≠ W545), Q700 (≠ S549), Q701 (≠ M550), C799 (≠ V670), N800 (= N671), T804 (≠ V675), Q807 (= Q678), S865 (≠ K739), G866 (= G740), V867 (≠ I741), G868 (= G742), E869 (= E743)
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
Query Sequence
>AZOBR_RS29690 FitnessBrowser__azobra:AZOBR_RS29690
MGEVSTAGSGAGSGVGARVRRKEDDRLLRGRGRFVGDIALVGMKELAFVRSPVAHATITG
IEIPEEHRGAVFTWADLAAGGVKPIRAVSGLPGFKVSEQPALADGKVRFVGEPVAVCVAA
TRAEAEDIAASVFVDYAELPVNSDMLEAVAPGAPKVHDHWPDNVFLETNVGGNIAEIAAT
APVKVSRTIRTARQCMVPLEGKGVVAHWDRHVEQLVLTTSTQMPHIVRAGLSECLDLDQG
LIRVVAPDVGGGFGWKGLLQPEEIVAAWIAMRLDRPVRWTEDRREHLVAAANAREHHYEI
TAYADARGRLLGIEADAWVDAGAYSVYPFSACLEAAQVGSILPGPYDFAHYRCRTFSVCT
NKPPIVPYRGVARTGVCFAMEQMIDAVADAVGREPWQVRLENLVPPEKMPFDNVTKKHFD
SGDYPESVRRAVAAIELEGWRARQKAGEADGRLIGVGFATYCEQSAHGTAVYHGWGIPMV
PGHEQAQARITPDGGLELRVGVQSHGQSMETTFAQVAHEVLGIPLEKIKLVHGDTGLTPY
STGTWGSRSMVMAGGAVATACRTLAERLRKIGAHLMQAGPDGVVLKDGAVTAGPAAVTIR
EIAHTWYRAPQLLPADVDRGGLEVTAGYKPGSDHGTFSYATHAVAVAVDPEIGQVEILDY
VVVEDAGTMVNPMVVDGQIYGGVAQGVGTALYERMPYDAEGQPLASTFADYLIPGFTEVP
HVRIIHMLTPSPYTEFGVKGIGEGGAIAPPAAICNAINDALKPLGVIVTNAPMTPEVILT
AIAGERGAA
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