SitesBLAST
Comparing 3609273 FitnessBrowser__Dino:3609273 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)
38% identity, 99% coverage: 6:788/791 of query aligns to 11:790/797 of 1ffvB
- active site: Q231 (= Q225), V266 (≠ I261), P343 (= P337), I349 (≠ L344), R378 (= R372), C379 (≠ G373), E751 (= E746), S752 (≠ A747)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G255), G261 (= G256), F262 (= F257), G263 (= G258), A376 (= A370), R378 (= R372), C379 (≠ G373), Q516 (≠ H508), G517 (= G509), Q518 (= Q510), H520 (= H512), T523 (≠ A515), Y556 (= Y548), G557 (= G549), S558 (= S550), S560 (= S552), T561 (≠ I553), C674 (≠ F668), I678 (= I672), I683 (≠ V677), Q686 (= Q680), K747 (= K742), G748 (= G743), V749 (≠ C744), A750 (≠ G745), E751 (= E746)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
38% identity, 99% coverage: 6:788/791 of query aligns to 11:790/797 of 1ffuB
- active site: Q231 (= Q225), V266 (≠ I261), P343 (= P337), I349 (≠ L344), R378 (= R372), C379 (≠ G373), E751 (= E746), S752 (≠ A747)
- binding cytidine-5'-diphosphate: Q518 (= Q510), H520 (= H512), T523 (≠ A515), S558 (= S550), S560 (= S552), T561 (≠ I553), C674 (≠ F668), T676 (≠ N670), I678 (= I672), I683 (≠ V677), K747 (= K742), G748 (= G743), V749 (≠ C744), A750 (≠ G745)
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)
38% identity, 99% coverage: 6:788/791 of query aligns to 17:796/803 of P19913
- R384 (= R372) modified: 4-hydroxyarginine
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
37% identity, 99% coverage: 6:785/791 of query aligns to 14:793/803 of 1n60B
- active site: Q234 (= Q225), V269 (≠ I261), P346 (≠ L340), I352 (≠ L344), R381 (= R372), C382 (≠ G373), E757 (= E746), S758 (≠ A747)
- binding pterin cytosine dinucleotide: G264 (= G256), F265 (= F257), R381 (= R372), Q522 (≠ H508), G523 (= G509), Q524 (= Q510), H526 (= H512), T529 (≠ A515), T561 (= T547), Y562 (= Y548), G563 (= G549), S564 (= S550), S566 (= S552), T567 (≠ I553), C680 (≠ F668), I684 (= I672), I688 (= I676), I689 (≠ V677), Q692 (= Q680), K753 (= K742), G754 (= G743), V755 (≠ C744), E757 (= E746)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F257), G266 (= G258), Y562 (= Y548), G563 (= G549), E757 (= E746)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
37% identity, 99% coverage: 6:785/791 of query aligns to 15:794/804 of 1n62B
- active site: Q235 (= Q225), V270 (≠ I261), P347 (≠ L340), I353 (≠ L344), R382 (= R372), C383 (≠ G373), E758 (= E746), S759 (≠ A747)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G258), V379 (vs. gap), A380 (= A370), R382 (= R372), C383 (≠ G373), F385 (≠ G375), Y563 (= Y548), G564 (= G549), E758 (= E746)
- binding pterin cytosine dinucleotide: G265 (= G256), F266 (= F257), R382 (= R372), Q523 (≠ H508), G524 (= G509), Q525 (= Q510), H527 (= H512), T530 (≠ A515), T562 (= T547), Y563 (= Y548), G564 (= G549), S565 (= S550), S567 (= S552), T568 (≠ I553), C681 (≠ F668), I685 (= I672), I689 (= I676), I690 (≠ V677), Q693 (= Q680), K754 (= K742), G755 (= G743), V756 (≠ C744), G757 (= G745), E758 (= E746)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
37% identity, 99% coverage: 6:785/791 of query aligns to 15:794/804 of 1n5wB
- active site: Q235 (= Q225), V270 (≠ I261), P347 (≠ L340), I353 (≠ L344), R382 (= R372), C383 (≠ G373), E758 (= E746), S759 (≠ A747)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G258), A380 (= A370), R382 (= R372), C383 (≠ G373), Y563 (= Y548), G564 (= G549), E758 (= E746)
- binding pterin cytosine dinucleotide: G265 (= G256), F266 (= F257), R382 (= R372), Q523 (≠ H508), G524 (= G509), Q525 (= Q510), H527 (= H512), T530 (≠ A515), T562 (= T547), Y563 (= Y548), S565 (= S550), S567 (= S552), T568 (≠ I553), C681 (≠ F668), I685 (= I672), I689 (= I676), I690 (≠ V677), Q693 (= Q680), K754 (= K742), G755 (= G743), V756 (≠ C744), E758 (= E746)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
37% identity, 99% coverage: 6:785/791 of query aligns to 15:794/804 of 1zxiB
- active site: Q235 (= Q225), V270 (≠ I261), P347 (≠ L340), I353 (≠ L344), R382 (= R372), C383 (≠ G373), E758 (= E746), S759 (≠ A747)
- binding copper (ii) ion: C383 (≠ G373), S384 (≠ A374), E758 (= E746)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F257), G267 (= G258), A380 (= A370), Y381 (= Y371), R382 (= R372), C383 (≠ G373), Y563 (= Y548), G564 (= G549), E758 (= E746)
- binding pterin cytosine dinucleotide: G265 (= G256), F266 (= F257), R382 (= R372), Q523 (≠ H508), G524 (= G509), Q525 (= Q510), H527 (= H512), T530 (≠ A515), T562 (= T547), Y563 (= Y548), S565 (= S550), S567 (= S552), T568 (≠ I553), C681 (≠ F668), I685 (= I672), I689 (= I676), I690 (≠ V677), Q693 (= Q680), K754 (= K742), G755 (= G743), V756 (≠ C744), E758 (= E746)
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
37% identity, 99% coverage: 6:785/791 of query aligns to 16:795/805 of 1n63B
- active site: Q236 (= Q225), V271 (≠ I261), P348 (≠ L340), I354 (≠ L344), R383 (= R372), C384 (≠ G373), E759 (= E746), S760 (≠ A747)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G258), A381 (= A370), R383 (= R372), C384 (≠ G373), Y564 (= Y548), G565 (= G549), E759 (= E746)
- binding pterin cytosine dinucleotide: G266 (= G256), F267 (= F257), R383 (= R372), Q524 (≠ H508), G525 (= G509), Q526 (= Q510), H528 (= H512), T531 (≠ A515), T563 (= T547), Y564 (= Y548), S566 (= S550), S568 (= S552), T569 (≠ I553), C682 (≠ F668), I686 (= I672), I690 (= I676), I691 (≠ V677), Q694 (= Q680), K755 (= K742), G756 (= G743), V757 (≠ C744), E759 (= E746)
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)
37% identity, 99% coverage: 6:785/791 of query aligns to 20:799/809 of P19919
- C388 (≠ G373) binding
- E763 (= E746) binding
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
37% identity, 100% coverage: 3:791/791 of query aligns to 10:785/786 of 1t3qB
- active site: Q224 (= Q225), A259 (≠ I261), E336 (≠ P337), V343 (≠ L344), R371 (= R372), E743 (= E746), S744 (≠ A747)
- binding pterin cytosine dinucleotide: G254 (= G256), F255 (= F257), R371 (= R372), S506 (≠ H508), G507 (= G509), Q508 (= Q510), H510 (= H512), T513 (≠ A515), Y545 (= Y548), S547 (= S550), G549 (≠ S552), A550 (≠ I553), C666 (≠ F668), I670 (= I672), I674 (= I676), V675 (= V677), Q678 (= Q680), K739 (= K742), G740 (= G743), M741 (≠ C744), G742 (= G745)
7dqxD Crystal structure of xanthine dehydrogenase family protein
34% identity, 94% coverage: 3:746/791 of query aligns to 2:728/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G255), S248 (≠ G256), F249 (= F257), R363 (= R372), V491 (≠ H508), G492 (= G509), Q493 (= Q510), G494 (= G511), V498 (≠ A515), S530 (≠ T547), W531 (≠ Y548), S532 (≠ G549), S533 (= S550), R534 (= R551), S535 (= S552), T536 (≠ I553), T658 (≠ I676), T659 (≠ V677), Q662 (= Q680), G725 (= G743), L726 (≠ C744), G727 (= G745), E728 (= E746)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
34% identity, 96% coverage: 7:766/791 of query aligns to 3:688/701 of 4zohA
- active site: Q186 (= Q225), I219 (= I261), V298 (≠ L340), S300 (≠ G342), M304 (≠ L344), R332 (= R372), E668 (= E746), A669 (= A747)
- binding pterin cytosine dinucleotide: G213 (= G255), A214 (≠ G256), F215 (= F257), R332 (= R372), H442 (= H508), G443 (= G509), Q444 (= Q510), D446 (≠ H512), W482 (≠ Y548), S484 (= S550), T486 (≠ S552), V487 (≠ I553), I594 (= I672), N595 (= N673), L598 (≠ I676), Q602 (= Q680), K664 (= K742), G665 (= G743), I666 (≠ C744), G667 (= G745), E668 (= E746)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
31% identity, 100% coverage: 1:791/791 of query aligns to 5:765/769 of O33819
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
31% identity, 99% coverage: 5:791/791 of query aligns to 1:757/761 of 1rm6A
- active site: Q206 (= Q225), T241 (≠ I261), Y318 (≠ H341), L322 (= L344), R350 (= R372), E718 (= E746), G719 (≠ A747)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G255), G236 (= G256), F237 (= F257), G238 (= G258), R350 (= R372), I473 (≠ H508), G474 (= G509), Q475 (= Q510), G476 (= G511), Y513 (= Y548), S514 (≠ G549), S515 (= S550), V517 (≠ S552), T518 (≠ I553), L646 (≠ I672), N647 (= N673), V651 (= V677), Q654 (= Q680), K714 (= K742), E715 (≠ G743), A716 (≠ C744), S717 (≠ G745), E718 (= E746)
1dgjA Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774 (see paper)
28% identity, 100% coverage: 1:788/791 of query aligns to 169:905/906 of 1dgjA
- active site: V391 (≠ Q225), F427 (≠ Y262), R503 (≠ L340), Y507 (≠ L344), R535 (= R372), E869 (= E746), M870 (≠ A747)
- binding molybdenum (iv)oxide: G424 (= G258), R535 (= R372), G698 (≠ Y548), E869 (= E746)
- binding pterin cytosine dinucleotide: F423 (= F257), G424 (= G258), R535 (= R372), W652 (≠ S505), H655 (= H508), G656 (= G509), Q657 (= Q510), G658 (= G511), A697 (≠ T547), G698 (≠ Y548), S700 (= S550), S702 (= S552), Q703 (≠ I553), C799 (≠ I672), N800 (= N673), V803 (≠ I676), V804 (= V677), Q807 (= Q680), S865 (≠ K742), G866 (= G743), V867 (≠ C744), G868 (= G745), E869 (= E746)
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)
28% identity, 100% coverage: 1:788/791 of query aligns to 169:905/907 of 4usaA
- active site: I390 (≠ P227), F425 (≠ Y262), R501 (≠ L340), F505 (≠ L344), R533 (= R372), E869 (= E746), L870 (≠ A747)
- binding bicarbonate ion: R460 (≠ G297), A531 (= A370), F532 (≠ Y371), Y535 (≠ A374), Q539 (≠ E378)
- binding hydrocinnamic acid: I255 (≠ H89), F425 (≠ Y262), F494 (= F332), L497 (≠ I336), Y535 (≠ A374), L626 (= L475)
- binding magnesium ion: E899 (≠ S782), E903 (≠ A786)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G256), F421 (= F257), G422 (= G258), R533 (= R372), W650 (≠ S505), H653 (= H508), G654 (= G509), Q655 (= Q510), G656 (= G511), S695 (≠ T547), G696 (≠ Y548), G697 (= G549), Q700 (≠ S552), Q701 (≠ I553), C799 (≠ I672), N800 (= N673), T804 (≠ V677), Q807 (= Q680), S865 (≠ K742), G866 (= G743), V867 (≠ C744), G868 (= G745), E869 (= E746)
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)
28% identity, 100% coverage: 1:788/791 of query aligns to 169:905/907 of 4us9A
- active site: I390 (≠ P227), F425 (≠ Y262), R501 (≠ L340), F505 (≠ L344), R533 (= R372), E869 (= E746), L870 (≠ A747)
- binding 3-phenylpropanal: I255 (≠ H89), F257 (≠ Q91), P258 (= P92), H752 (≠ K600)
- binding bicarbonate ion: R460 (≠ G297), L498 (≠ P337), A531 (= A370), F532 (≠ Y371), Y535 (≠ A374), Q539 (≠ E378), R890 (≠ T773), Y892 (≠ I775)
- binding magnesium ion: E899 (≠ S782), E903 (≠ A786)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G256), F421 (= F257), G422 (= G258), R533 (= R372), W650 (≠ S505), H653 (= H508), G654 (= G509), Q655 (= Q510), G656 (= G511), S695 (≠ T547), G696 (≠ Y548), G697 (= G549), Q700 (≠ S552), Q701 (≠ I553), C799 (≠ I672), N800 (= N673), T804 (≠ V677), Q807 (= Q680), S865 (≠ K742), G866 (= G743), V867 (≠ C744), G868 (= G745), E869 (= E746)
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)
28% identity, 100% coverage: 1:788/791 of query aligns to 169:905/907 of 4us8A
- active site: I390 (≠ P227), F425 (≠ Y262), R501 (≠ L340), F505 (≠ L344), R533 (= R372), E869 (= E746), L870 (≠ A747)
- binding bicarbonate ion: R460 (≠ G297), L498 (≠ P337), A531 (= A370), F532 (≠ Y371), Y535 (≠ A374), Q539 (≠ E378)
- binding benzaldehyde: I255 (≠ H89), I255 (≠ H89), L394 (≠ I230), F425 (≠ Y262), F425 (≠ Y262), F425 (≠ Y262), F425 (≠ Y262), L497 (≠ I336), L497 (≠ I336), R501 (≠ L340), A531 (= A370), Y535 (≠ A374), Y535 (≠ A374), L626 (= L475), L626 (= L475), L626 (= L475), P694 (≠ G546), G696 (≠ Y548), G697 (= G549)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G256), F421 (= F257), G422 (= G258), R533 (= R372), H653 (= H508), G654 (= G509), Q655 (= Q510), G656 (= G511), S695 (≠ T547), G696 (≠ Y548), G697 (= G549), Q700 (≠ S552), Q701 (≠ I553), C799 (≠ I672), N800 (= N673), T804 (≠ V677), Q807 (= Q680), S865 (≠ K742), G866 (= G743), V867 (≠ C744), G868 (= G745), E869 (= E746)
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, 100% coverage: 1:788/791 of query aligns to 169:905/907 of 4c7yA
- active site: I390 (≠ P227), F425 (≠ Y262), R501 (≠ L340), F505 (≠ L344), R533 (= R372), E869 (= E746), L870 (≠ A747)
- binding bicarbonate ion: R460 (≠ G297), L498 (≠ P337), A531 (= A370), Y535 (≠ A374), Q539 (≠ E378)
- binding magnesium ion: E899 (≠ S782), E903 (≠ A786)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G256), F421 (= F257), G422 (= G258), R533 (= R372), W650 (≠ S505), H653 (= H508), G654 (= G509), Q655 (= Q510), G656 (= G511), S695 (≠ T547), G696 (≠ Y548), Q700 (≠ S552), Q701 (≠ I553), C799 (≠ I672), N800 (= N673), T804 (≠ V677), Q807 (= Q680), S865 (≠ K742), G866 (= G743), V867 (≠ C744), G868 (= G745), E869 (= E746)
- binding hydrogen peroxide: G696 (≠ Y548), G697 (= G549), E869 (= E746)
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)
28% identity, 100% coverage: 1:788/791 of query aligns to 169:905/907 of 3fc4A
- active site: I390 (≠ P227), F425 (≠ Y262), R501 (≠ L340), F505 (≠ L344), R533 (= R372), E869 (= E746), L870 (≠ A747)
- binding 1,2-ethanediol: Y535 (≠ A374), Y622 (≠ A471), G696 (≠ Y548), G697 (= G549), E869 (= E746)
- binding magnesium ion: E899 (≠ S782), E903 (≠ A786)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G419 (= G255), T420 (≠ G256), F421 (= F257), G422 (= G258), R533 (= R372), W650 (≠ S505), H653 (= H508), G654 (= G509), Q655 (= Q510), G656 (= G511), S695 (≠ T547), G696 (≠ Y548), Q700 (≠ S552), Q701 (≠ I553), C799 (≠ I672), N800 (= N673), T804 (≠ V677), Q807 (= Q680), S865 (≠ K742), G866 (= G743), V867 (≠ C744), G868 (= G745), E869 (= E746)
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
>3609273 FitnessBrowser__Dino:3609273
MPKDGGIGASSKRREDVRFLTGRGRYTDDINLNNQTYAYFLRSEVAHGKINGIDTAAAEG
MDGVIRVFTAKDFEGVGGVPCGWQVTDIHGQPMKEPKHPVLAEGKVRHVGDPIAVVVAES
LEQARDAAEAIELDIEELPAVMDMKAALAEGATKVHDDLDDNLCYEWGFVEENRAAVDEA
IKNAHHVTTLELTNNRLVANPMEPRVAVGDYHPGTQDYTLYTTSQNPHVIRLLMGAFVLG
IPEHKLRVVAPDVGGGFGSKIYHYAEEAFVTFASGQIGRPVKWTSSRSEAFVSDAHGRDH
VTKIELALDENHKFTALRCDTYANMGAYLSTFAPSIPTWLHGTLLAGNYTTPLIYTNVKA
VFTTTTPVDAYRGAGRPEATFQLERVVDKAARELGVDPAELRRINFIKPEQFPYDTPVAV
TYDTGNYHATLEKGLEMAGADTFEARAAESKARGKLRGFGLAHFIEACGIAPSNLVGQLG
ARAGLYESATVRVNATGSISVMTGSHSHGQGHETAFPQVVAEMLGIDENMIEIVHGDTAN
TPMGMGTYGSRSIAVGGSAMVRATEKIINKAKKIAAHLLEAAEGDIELKDGAFTVAGTDK
SVAWGDVTLAAYVPHNYPLEDIEPGLEETAFYDPSNFTYPSGAYICEVEVDPDTGKVDVL
AFTAADDFGNVINPMIVEGQVHGGVAQGIGQALLENCSYDADGQLLSGSYMDYTMPRADD
LPMFEVDHSCITPCTHNPLGVKGCGEAGAIGSPPAVVNAVIDALHRAGQTHVTHIDMPLT
PSRVWAAIHGK
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