SitesBLAST
Comparing 3607631 FitnessBrowser__Dino:3607631 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)
1ffvB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava (see paper)
33% identity, 98% coverage: 8:757/763 of query aligns to 12:791/797 of 1ffvB
- active site: Q231 (= Q220), V266 (≠ N255), P343 (≠ T332), I349 (≠ L338), R378 (= R365), C379 (≠ G366), E751 (= E717), S752 (= S718)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G249), G261 (≠ S250), F262 (= F251), G263 (= G252), A376 (vs. gap), R378 (= R365), C379 (≠ G366), Q516 (≠ A492), G517 (= G493), Q518 (= Q494), H520 (= H496), T523 (≠ A499), Y556 (≠ F531), G557 (= G532), S558 (= S533), S560 (≠ T535), T561 (≠ M536), C674 (≠ V640), I678 (= I644), I683 (≠ V649), Q686 (= Q652), K747 (= K713), G748 (= G714), V749 (≠ A715), A750 (≠ G716), E751 (= E717)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
33% identity, 98% coverage: 8:757/763 of query aligns to 12:791/797 of 1ffuB
- active site: Q231 (= Q220), V266 (≠ N255), P343 (≠ T332), I349 (≠ L338), R378 (= R365), C379 (≠ G366), E751 (= E717), S752 (= S718)
- binding cytidine-5'-diphosphate: Q518 (= Q494), H520 (= H496), T523 (≠ A499), S558 (= S533), S560 (≠ T535), T561 (≠ M536), C674 (≠ V640), T676 (= T642), I678 (= I644), I683 (≠ V649), K747 (= K713), G748 (= G714), V749 (≠ A715), A750 (≠ G716)
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)
33% identity, 97% coverage: 16:757/763 of query aligns to 26:797/803 of P19913
- R384 (= R365) modified: 4-hydroxyarginine
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
32% identity, 98% coverage: 9:753/763 of query aligns to 18:795/805 of 1n63B
- active site: Q236 (= Q220), V271 (≠ N255), P348 (= P336), I354 (vs. gap), R383 (= R365), C384 (≠ G366), E759 (= E717), S760 (= S718)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G252), A381 (≠ P363), R383 (= R365), C384 (≠ G366), Y564 (≠ F531), G565 (= G532), E759 (= E717)
- binding pterin cytosine dinucleotide: G266 (≠ S250), F267 (= F251), R383 (= R365), Q524 (≠ A492), G525 (= G493), Q526 (= Q494), H528 (= H496), T531 (≠ A499), T563 (= T530), Y564 (≠ F531), S566 (= S533), S568 (≠ T535), T569 (≠ M536), C682 (≠ V640), I686 (= I644), I690 (≠ L648), I691 (≠ V649), Q694 (= Q652), K755 (= K713), G756 (= G714), V757 (≠ A715), E759 (= E717)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
32% identity, 98% coverage: 9:753/763 of query aligns to 17:794/804 of 1n62B
- active site: Q235 (= Q220), V270 (≠ N255), P347 (= P336), I353 (vs. gap), R382 (= R365), C383 (≠ G366), E758 (= E717), S759 (= S718)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G252), V379 (≠ A362), A380 (≠ P363), R382 (= R365), C383 (≠ G366), F385 (≠ G368), Y563 (≠ F531), G564 (= G532), E758 (= E717)
- binding pterin cytosine dinucleotide: G265 (≠ S250), F266 (= F251), R382 (= R365), Q523 (≠ A492), G524 (= G493), Q525 (= Q494), H527 (= H496), T530 (≠ A499), T562 (= T530), Y563 (≠ F531), G564 (= G532), S565 (= S533), S567 (≠ T535), T568 (≠ M536), C681 (≠ V640), I685 (= I644), I689 (≠ L648), I690 (≠ V649), Q693 (= Q652), K754 (= K713), G755 (= G714), V756 (≠ A715), G757 (= G716), E758 (= E717)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
32% identity, 98% coverage: 9:753/763 of query aligns to 17:794/804 of 1n5wB
- active site: Q235 (= Q220), V270 (≠ N255), P347 (= P336), I353 (vs. gap), R382 (= R365), C383 (≠ G366), E758 (= E717), S759 (= S718)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G252), A380 (≠ P363), R382 (= R365), C383 (≠ G366), Y563 (≠ F531), G564 (= G532), E758 (= E717)
- binding pterin cytosine dinucleotide: G265 (≠ S250), F266 (= F251), R382 (= R365), Q523 (≠ A492), G524 (= G493), Q525 (= Q494), H527 (= H496), T530 (≠ A499), T562 (= T530), Y563 (≠ F531), S565 (= S533), S567 (≠ T535), T568 (≠ M536), C681 (≠ V640), I685 (= I644), I689 (≠ L648), I690 (≠ V649), Q693 (= Q652), K754 (= K713), G755 (= G714), V756 (≠ A715), E758 (= E717)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
32% identity, 98% coverage: 9:753/763 of query aligns to 17:794/804 of 1zxiB
- active site: Q235 (= Q220), V270 (≠ N255), P347 (= P336), I353 (vs. gap), R382 (= R365), C383 (≠ G366), E758 (= E717), S759 (= S718)
- binding copper (ii) ion: C383 (≠ G366), S384 (≠ A367), E758 (= E717)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F251), G267 (= G252), A380 (≠ P363), Y381 (= Y364), R382 (= R365), C383 (≠ G366), Y563 (≠ F531), G564 (= G532), E758 (= E717)
- binding pterin cytosine dinucleotide: G265 (≠ S250), F266 (= F251), R382 (= R365), Q523 (≠ A492), G524 (= G493), Q525 (= Q494), H527 (= H496), T530 (≠ A499), T562 (= T530), Y563 (≠ F531), S565 (= S533), S567 (≠ T535), T568 (≠ M536), C681 (≠ V640), I685 (= I644), I689 (≠ L648), I690 (≠ V649), Q693 (= Q652), K754 (= K713), G755 (= G714), V756 (≠ A715), E758 (= E717)
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)
32% identity, 98% coverage: 9:753/763 of query aligns to 22:799/809 of P19919
- C388 (≠ G366) binding
- E763 (= E717) binding
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
32% identity, 98% coverage: 9:753/763 of query aligns to 16:793/803 of 1n60B
- active site: Q234 (= Q220), V269 (≠ N255), P346 (= P336), I352 (vs. gap), R381 (= R365), C382 (≠ G366), E757 (= E717), S758 (= S718)
- binding pterin cytosine dinucleotide: G264 (≠ S250), F265 (= F251), R381 (= R365), Q522 (≠ A492), G523 (= G493), Q524 (= Q494), H526 (= H496), T529 (≠ A499), T561 (= T530), Y562 (≠ F531), G563 (= G532), S564 (= S533), S566 (≠ T535), T567 (≠ M536), C680 (≠ V640), I684 (= I644), I688 (≠ L648), I689 (≠ V649), Q692 (= Q652), K753 (= K713), G754 (= G714), V755 (≠ A715), E757 (= E717)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F251), G266 (= G252), Y562 (≠ F531), G563 (= G532), E757 (= E717)
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
33% identity, 99% coverage: 1:757/763 of query aligns to 7:783/786 of 1t3qB
- active site: Q224 (= Q220), A259 (≠ N255), E336 (≠ T332), V343 (vs. gap), R371 (= R365), E743 (= E717), S744 (= S718)
- binding pterin cytosine dinucleotide: G254 (≠ S250), F255 (= F251), R371 (= R365), S506 (≠ A492), G507 (= G493), Q508 (= Q494), H510 (= H496), T513 (≠ A499), Y545 (≠ F531), S547 (= S533), G549 (= G540), A550 (= A541), C666 (≠ V640), I670 (= I644), I674 (≠ L648), V675 (= V649), Q678 (= Q652), K739 (= K713), G740 (= G714), M741 (≠ A715), G742 (= G716)
7dqxD Crystal structure of xanthine dehydrogenase family protein
31% identity, 93% coverage: 8:717/763 of query aligns to 6:728/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G249), S248 (= S250), F249 (= F251), R363 (= R365), V491 (≠ A492), G492 (= G493), Q493 (= Q494), G494 (= G495), V498 (≠ A499), S530 (≠ T530), W531 (≠ F531), S532 (≠ G532), S533 (= S533), R534 (= R534), S535 (≠ T535), T536 (≠ M536), T658 (≠ L648), T659 (≠ V649), Q662 (= Q652), G725 (= G714), L726 (≠ A715), G727 (= G716), E728 (= E717)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
32% identity, 97% coverage: 8:748/763 of query aligns to 3:696/701 of 4zohA
- active site: Q186 (= Q220), I219 (≠ N255), V298 (≠ M331), S300 (= S333), M304 (≠ G337), R332 (= R365), E668 (= E717), A669 (≠ S718)
- binding pterin cytosine dinucleotide: G213 (= G249), A214 (≠ S250), F215 (= F251), R332 (= R365), H442 (≠ A492), G443 (= G493), Q444 (= Q494), D446 (≠ H496), W482 (≠ F531), S484 (= S533), T486 (= T535), V487 (≠ M543), I594 (= I644), N595 (= N645), L598 (= L648), Q602 (= Q652), K664 (= K713), G665 (= G714), I666 (≠ A715), G667 (= G716), E668 (= E717)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
29% identity, 97% coverage: 21:757/763 of query aligns to 16:755/761 of 1rm6A
- active site: Q206 (= Q220), T241 (≠ N255), Y318 (≠ P336), L322 (vs. gap), R350 (= R365), E718 (= E717), G719 (≠ S718)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G249), G236 (≠ S250), F237 (= F251), G238 (= G252), R350 (= R365), I473 (≠ A492), G474 (= G493), Q475 (= Q494), G476 (= G495), Y513 (≠ F531), S514 (≠ G532), S515 (= S533), V517 (≠ T535), T518 (≠ M536), L646 (≠ I644), N647 (= N645), V651 (= V649), Q654 (= Q652), K714 (= K713), E715 (≠ G714), A716 (= A715), S717 (≠ G716), E718 (= E717)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
29% identity, 97% coverage: 21:757/763 of query aligns to 24:763/769 of O33819
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
27% identity, 96% coverage: 8:736/763 of query aligns to 7:734/748 of 5y6qC
- active site: Q204 (= Q220), P239 (≠ N255), A310 (= A317), V316 (≠ M323), R344 (= R365), E715 (= E717), L716 (≠ S718)
- binding pterin cytosine dinucleotide: G233 (= G249), G234 (≠ S250), F235 (= F251), I461 (≠ A492), G462 (= G493), T463 (≠ Q494), G464 (= G495), I468 (≠ A499), G500 (≠ F531), S502 (= S533), Q503 (≠ R534), L504 (≠ T535), A505 (≠ M536), R638 (≠ T642), Y640 (≠ I644), N641 (= N645), Q648 (= Q652), K711 (= K713), V713 (≠ A715), G714 (= G716), E715 (= E717)
4usaA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with trans-cinnamaldehyde (see paper)
25% identity, 95% coverage: 35:757/763 of query aligns to 206:906/907 of 4usaA
- active site: I390 (≠ Q220), F425 (≠ N255), R501 (≠ N334), F505 (≠ L338), R533 (= R365), E869 (= E717), L870 (≠ S718)
- binding bicarbonate ion: R460 (≠ S291), A531 (≠ P363), F532 (≠ Y364), Y535 (≠ A367), Q539 (≠ E371)
- binding hydrocinnamic acid: I255 (≠ R78), F425 (≠ N255), F494 (≠ M323), L497 (≠ M326), Y535 (≠ A367), L626 (vs. gap)
- binding magnesium ion: E899 (≠ H750), E903 (≠ A754)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ S250), F421 (= F251), G422 (= G252), R533 (= R365), W650 (≠ A489), H653 (≠ A492), G654 (= G493), Q655 (= Q494), G656 (= G495), S695 (≠ T530), G696 (≠ F531), G697 (= G532), Q700 (≠ T535), Q701 (≠ M536), C799 (≠ I644), N800 (= N645), T804 (≠ V649), Q807 (= Q652), S865 (≠ K713), G866 (= G714), V867 (≠ A715), G868 (= G716), E869 (= E717)
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)
25% identity, 95% coverage: 35:757/763 of query aligns to 206:906/907 of 4us9A
- active site: I390 (≠ Q220), F425 (≠ N255), R501 (≠ N334), F505 (≠ L338), R533 (= R365), E869 (= E717), L870 (≠ S718)
- binding 3-phenylpropanal: I255 (≠ R78), F257 (= F80), P258 (= P81), H752 (≠ E589)
- binding bicarbonate ion: R460 (≠ S291), L498 (≠ M331), A531 (≠ P363), F532 (≠ Y364), Y535 (≠ A367), Q539 (≠ E371), R890 (= R741), Y892 (≠ L743)
- binding magnesium ion: E899 (≠ H750), E903 (≠ A754)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ S250), F421 (= F251), G422 (= G252), R533 (= R365), W650 (≠ A489), H653 (≠ A492), G654 (= G493), Q655 (= Q494), G656 (= G495), S695 (≠ T530), G696 (≠ F531), G697 (= G532), Q700 (≠ T535), Q701 (≠ M536), C799 (≠ I644), N800 (= N645), T804 (≠ V649), Q807 (= Q652), S865 (≠ K713), G866 (= G714), V867 (≠ A715), G868 (= G716), E869 (= E717)
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)
25% identity, 95% coverage: 35:757/763 of query aligns to 206:906/907 of 4us8A
- active site: I390 (≠ Q220), F425 (≠ N255), R501 (≠ N334), F505 (≠ L338), R533 (= R365), E869 (= E717), L870 (≠ S718)
- binding bicarbonate ion: R460 (≠ S291), L498 (≠ M331), A531 (≠ P363), F532 (≠ Y364), Y535 (≠ A367), Q539 (≠ E371)
- binding benzaldehyde: I255 (≠ R78), I255 (≠ R78), L394 (≠ R224), F425 (≠ N255), F425 (≠ N255), F425 (≠ N255), F425 (≠ N255), L497 (≠ M326), L497 (≠ M326), R501 (≠ N334), A531 (≠ P363), Y535 (≠ A367), Y535 (≠ A367), L626 (vs. gap), L626 (vs. gap), L626 (vs. gap), P694 (≠ G529), G696 (≠ F531), G697 (= G532)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ S250), F421 (= F251), G422 (= G252), R533 (= R365), H653 (≠ A492), G654 (= G493), Q655 (= Q494), G656 (= G495), S695 (≠ T530), G696 (≠ F531), G697 (= G532), Q700 (≠ T535), Q701 (≠ M536), C799 (≠ I644), N800 (= N645), T804 (≠ V649), Q807 (= Q652), S865 (≠ K713), G866 (= G714), V867 (≠ A715), G868 (= G716), E869 (= E717)
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)
25% identity, 95% coverage: 35:757/763 of query aligns to 206:906/907 of 4c7yA
- active site: I390 (≠ Q220), F425 (≠ N255), R501 (≠ N334), F505 (≠ L338), R533 (= R365), E869 (= E717), L870 (≠ S718)
- binding bicarbonate ion: R460 (≠ S291), L498 (≠ M331), A531 (≠ P363), Y535 (≠ A367), Q539 (≠ E371)
- binding magnesium ion: E899 (≠ H750), E903 (≠ A754)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ S250), F421 (= F251), G422 (= G252), R533 (= R365), W650 (≠ A489), H653 (≠ A492), G654 (= G493), Q655 (= Q494), G656 (= G495), S695 (≠ T530), G696 (≠ F531), Q700 (≠ T535), Q701 (≠ M536), C799 (≠ I644), N800 (= N645), T804 (≠ V649), Q807 (= Q652), S865 (≠ K713), G866 (= G714), V867 (≠ A715), G868 (= G716), E869 (= E717)
- binding hydrogen peroxide: G696 (≠ F531), G697 (= G532), E869 (= E717)
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)
25% identity, 95% coverage: 35:757/763 of query aligns to 206:906/907 of 3fc4A
- active site: I390 (≠ Q220), F425 (≠ N255), R501 (≠ N334), F505 (≠ L338), R533 (= R365), E869 (= E717), L870 (≠ S718)
- binding 1,2-ethanediol: Y535 (≠ A367), Y622 (≠ E459), G696 (≠ F531), G697 (= G532), E869 (= E717)
- binding magnesium ion: E899 (≠ H750), E903 (≠ A754)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G419 (= G249), T420 (≠ S250), F421 (= F251), G422 (= G252), R533 (= R365), W650 (≠ A489), H653 (≠ A492), G654 (= G493), Q655 (= Q494), G656 (= G495), S695 (≠ T530), G696 (≠ F531), Q700 (≠ T535), Q701 (≠ M536), C799 (≠ I644), N800 (= N645), T804 (≠ V649), Q807 (= Q652), S865 (≠ K713), G866 (= G714), V867 (≠ A715), G868 (= G716), E869 (= E717)
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
>3607631 FitnessBrowser__Dino:3607631
MARPETRFGTAQTRDEDGRLVRGAGCFVADVPAEGALWMEVVRSPYPAGRITALDLDAAR
AMPGVVCVLSGADQAGLRPFPLRYVPKGCDVVPTPFLPMATDRVTWVGEPVAVVVAETAG
QASDAADAVVLEVAEAPVVTDARTGAAPEAPRVWPDRDSNIAFTYELGDRDAFEAAAARA
AHVTRARIEISRVAAMTLEPRGALATCSPEGHMTLWTGTQAPHRVQGELAHVLDLPLDRI
RVRKTDTGGSFGMRNGAFPEDALALLAARATGRPVHWQGTRSEGFLADTASREQSVDAAL
ALDADGTFLALQVDGYAPIGAQMGQMSGHPMTSNLPGLAGVYRTPVIHAVMRGVHVNAMH
MAPYRGAGRPEAIYVIERMVELAAAETGRDPVALRLRNMIGPDQMPWATPHGFTYDSGDF
PTALRAALAGADAAGFAARREAARARGRLRGLGIACAIEPAGGGPKGAQLPEYAQLIAGP
EGLEIRTGAGDAGQGHATAFAQIAERLLGWRGPVTVRGGDTGEIARGTGTFGSRTMGSVG
AAMQAGSAQILEAARPEAADLLEVAARDLVFAQGAFRVAGTDRAIPLAEVTARTGRTFTA
EAFVATEAGTFPNGAHVAEVEVDPDTGAVQLAAYTVADDVGTVINPLLVEGQVHGGVAQG
LGQALMERIVHDADAALLTGSLMDYAVPRATDLCRIEVLHTPTPTTANPLGVKGAGESGT
VGALAAVMNAVCDAIGPEAARRLQMPASPHRVWAALNPTKEET
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