SitesBLAST
Comparing H281DRAFT_02182 FitnessBrowser__Burk376:H281DRAFT_02182 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1ffvB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava (see paper)
39% identity, 98% coverage: 10:787/795 of query aligns to 12:790/797 of 1ffvB
- active site: Q231 (= Q228), V266 (≠ I264), P343 (≠ Y344), I349 (vs. gap), R378 (= R375), C379 (≠ G376), E751 (= E748), S752 (≠ A749)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G258), G261 (= G259), F262 (= F260), G263 (= G261), A376 (= A373), R378 (= R375), C379 (≠ G376), Q516 (≠ H509), G517 (= G510), Q518 (= Q511), H520 (= H513), T523 (= T516), Y556 (= Y549), G557 (= G550), S558 (= S551), S560 (= S553), T561 (≠ I554), C674 (≠ F669), I678 (= I673), I683 (≠ V678), Q686 (= Q681), K747 (= K744), G748 (= G745), V749 (≠ C746), A750 (≠ G747), E751 (= E748)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
39% identity, 98% coverage: 10:787/795 of query aligns to 12:790/797 of 1ffuB
- active site: Q231 (= Q228), V266 (≠ I264), P343 (≠ Y344), I349 (vs. gap), R378 (= R375), C379 (≠ G376), E751 (= E748), S752 (≠ A749)
- binding cytidine-5'-diphosphate: Q518 (= Q511), H520 (= H513), T523 (= T516), S558 (= S551), S560 (= S553), T561 (≠ I554), C674 (≠ F669), T676 (≠ N671), I678 (= I673), I683 (≠ V678), K747 (= K744), G748 (= G745), V749 (≠ C746), A750 (≠ G747)
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)
39% identity, 97% coverage: 17:787/795 of query aligns to 25:796/803 of P19913
- R384 (= R375) modified: 4-hydroxyarginine
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
39% identity, 98% coverage: 10:785/795 of query aligns to 16:795/804 of 1zxiB
- active site: Q235 (= Q228), V270 (≠ I264), P347 (≠ T341), I353 (≠ L347), R382 (= R375), C383 (≠ G376), E758 (= E748), S759 (≠ A749)
- binding copper (ii) ion: C383 (≠ G376), S384 (≠ A377), E758 (= E748)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F260), G267 (= G261), A380 (= A373), Y381 (= Y374), R382 (= R375), C383 (≠ G376), Y563 (= Y549), G564 (= G550), E758 (= E748)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R375), Q523 (≠ H509), G524 (= G510), Q525 (= Q511), H527 (= H513), T530 (= T516), T562 (= T548), Y563 (= Y549), S565 (= S551), S567 (= S553), T568 (≠ I554), C681 (≠ F669), I685 (= I673), I689 (= I677), I690 (≠ V678), Q693 (= Q681), K754 (= K744), G755 (= G745), V756 (≠ C746), E758 (= E748)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
39% identity, 98% coverage: 10:785/795 of query aligns to 16:795/804 of 1n62B
- active site: Q235 (= Q228), V270 (≠ I264), P347 (≠ T341), I353 (≠ L347), R382 (= R375), C383 (≠ G376), E758 (= E748), S759 (≠ A749)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G261), V379 (vs. gap), A380 (= A373), R382 (= R375), C383 (≠ G376), F385 (≠ G378), Y563 (= Y549), G564 (= G550), E758 (= E748)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R375), Q523 (≠ H509), G524 (= G510), Q525 (= Q511), H527 (= H513), T530 (= T516), T562 (= T548), Y563 (= Y549), G564 (= G550), S565 (= S551), S567 (= S553), T568 (≠ I554), C681 (≠ F669), I685 (= I673), I689 (= I677), I690 (≠ V678), Q693 (= Q681), K754 (= K744), G755 (= G745), V756 (≠ C746), G757 (= G747), E758 (= E748)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
39% identity, 98% coverage: 10:785/795 of query aligns to 16:795/804 of 1n5wB
- active site: Q235 (= Q228), V270 (≠ I264), P347 (≠ T341), I353 (≠ L347), R382 (= R375), C383 (≠ G376), E758 (= E748), S759 (≠ A749)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G261), A380 (= A373), R382 (= R375), C383 (≠ G376), Y563 (= Y549), G564 (= G550), E758 (= E748)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R375), Q523 (≠ H509), G524 (= G510), Q525 (= Q511), H527 (= H513), T530 (= T516), T562 (= T548), Y563 (= Y549), S565 (= S551), S567 (= S553), T568 (≠ I554), C681 (≠ F669), I685 (= I673), I689 (= I677), I690 (≠ V678), Q693 (= Q681), K754 (= K744), G755 (= G745), V756 (≠ C746), E758 (= E748)
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
39% identity, 98% coverage: 10:785/795 of query aligns to 17:796/805 of 1n63B
- active site: Q236 (= Q228), V271 (≠ I264), P348 (≠ T341), I354 (≠ L347), R383 (= R375), C384 (≠ G376), E759 (= E748), S760 (≠ A749)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G261), A381 (= A373), R383 (= R375), C384 (≠ G376), Y564 (= Y549), G565 (= G550), E759 (= E748)
- binding pterin cytosine dinucleotide: G266 (= G259), F267 (= F260), R383 (= R375), Q524 (≠ H509), G525 (= G510), Q526 (= Q511), H528 (= H513), T531 (= T516), T563 (= T548), Y564 (= Y549), S566 (= S551), S568 (= S553), T569 (≠ I554), C682 (≠ F669), I686 (= I673), I690 (= I677), I691 (≠ V678), Q694 (= Q681), K755 (= K744), G756 (= G745), V757 (≠ C746), E759 (= E748)
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)
39% identity, 98% coverage: 10:785/795 of query aligns to 21:800/809 of P19919
- C388 (≠ G376) binding
- E763 (= E748) binding
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
39% identity, 98% coverage: 10:785/795 of query aligns to 15:794/803 of 1n60B
- active site: Q234 (= Q228), V269 (≠ I264), P346 (≠ T341), I352 (≠ L347), R381 (= R375), C382 (≠ G376), E757 (= E748), S758 (≠ A749)
- binding pterin cytosine dinucleotide: G264 (= G259), F265 (= F260), R381 (= R375), Q522 (≠ H509), G523 (= G510), Q524 (= Q511), H526 (= H513), T529 (= T516), T561 (= T548), Y562 (= Y549), G563 (= G550), S564 (= S551), S566 (= S553), T567 (≠ I554), C680 (≠ F669), I684 (= I673), I688 (= I677), I689 (≠ V678), Q692 (= Q681), K753 (= K744), G754 (= G745), V755 (≠ C746), E757 (= E748)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F260), G266 (= G261), Y562 (= Y549), G563 (= G550), E757 (= E748)
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
37% identity, 98% coverage: 10:788/795 of query aligns to 14:783/786 of 1t3qB
- active site: Q224 (= Q228), A259 (≠ I264), E336 (≠ P340), V343 (≠ L347), R371 (= R375), E743 (= E748), S744 (≠ A749)
- binding pterin cytosine dinucleotide: G254 (= G259), F255 (= F260), R371 (= R375), S506 (≠ H509), G507 (= G510), Q508 (= Q511), H510 (= H513), T513 (= T516), Y545 (= Y549), S547 (= S551), G549 (≠ S553), A550 (≠ I554), C666 (≠ F669), I670 (= I673), I674 (= I677), V675 (= V678), Q678 (= Q681), K739 (= K744), G740 (= G745), M741 (≠ C746), G742 (= G747)
7dqxD Crystal structure of xanthine dehydrogenase family protein
35% identity, 98% coverage: 7:785/795 of query aligns to 3:764/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G258), S248 (≠ G259), F249 (= F260), R363 (= R375), V491 (≠ H509), G492 (= G510), Q493 (= Q511), G494 (= G512), V498 (≠ T516), S530 (≠ T548), W531 (≠ Y549), S532 (≠ G550), S533 (= S551), R534 (= R552), S535 (= S553), T536 (≠ I554), T658 (≠ I677), T659 (≠ V678), Q662 (= Q681), G725 (= G745), L726 (≠ C746), G727 (= G747), E728 (= E748)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
35% identity, 95% coverage: 10:762/795 of query aligns to 3:682/701 of 4zohA
- active site: Q186 (= Q228), I219 (= I264), V298 (≠ L343), S300 (≠ A345), M304 (≠ L347), R332 (= R375), E668 (= E748), A669 (= A749)
- binding pterin cytosine dinucleotide: G213 (= G258), A214 (≠ G259), F215 (= F260), R332 (= R375), H442 (= H509), G443 (= G510), Q444 (= Q511), D446 (≠ H513), W482 (≠ Y549), S484 (= S551), T486 (≠ S553), V487 (≠ I554), I594 (= I673), N595 (= N674), L598 (≠ I677), Q602 (= Q681), K664 (= K744), G665 (= G745), I666 (≠ C746), G667 (= G747), E668 (= E748)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
31% identity, 99% coverage: 7:794/795 of query aligns to 8:769/769 of O33819
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
31% identity, 97% coverage: 23:794/795 of query aligns to 16:761/761 of 1rm6A
- active site: Q206 (= Q228), T241 (≠ I264), Y318 (= Y344), L322 (= L347), R350 (= R375), E718 (= E748), G719 (≠ A749)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G258), G236 (= G259), F237 (= F260), G238 (= G261), R350 (= R375), I473 (≠ H509), G474 (= G510), Q475 (= Q511), G476 (= G512), Y513 (= Y549), S514 (≠ G550), S515 (= S551), V517 (≠ S553), T518 (≠ I554), L646 (≠ I673), N647 (= N674), V651 (= V678), Q654 (= Q681), K714 (= K744), E715 (≠ G745), A716 (≠ C746), S717 (≠ G747), E718 (= E748)
Q8GUQ8 Xanthine dehydrogenase 1; AtXDH1; EC 1.17.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 96% coverage: 23:783/795 of query aligns to 611:1338/1361 of Q8GUQ8
- E831 (vs. gap) mutation to A: Loss of activity.
- R909 (≠ T341) mutation to A: Decreases activity 12-fold.
- E1297 (≠ S754) mutation to A: Decreases activity 40-fold.
Sites not aligning to the query:
- 364 W→A: Decreases activity 8-fold.
- 421 Y→A: Decreases activity 4-fold.
1dgjA Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774 (see paper)
25% identity, 99% coverage: 4:787/795 of query aligns to 170:905/906 of 1dgjA
- active site: V391 (≠ Q228), F427 (= F265), R503 (≠ L343), Y507 (≠ L347), R535 (= R375), E869 (= E748), M870 (≠ A749)
- binding molybdenum (iv)oxide: G424 (= G261), R535 (= R375), G698 (≠ Y549), E869 (= E748)
- binding pterin cytosine dinucleotide: F423 (= F260), G424 (= G261), R535 (= R375), W652 (≠ S506), H655 (= H509), G656 (= G510), Q657 (= Q511), G658 (= G512), A697 (≠ T548), G698 (≠ Y549), S700 (= S551), S702 (= S553), Q703 (≠ I554), C799 (≠ I673), N800 (= N674), V803 (≠ I677), V804 (= V678), Q807 (= Q681), S865 (≠ K744), G866 (= G745), V867 (≠ C746), G868 (= G747), E869 (= E748)
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
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
26% identity, 95% coverage: 10:765/795 of query aligns to 7:732/748 of 5y6qC
- active site: Q204 (= Q228), P239 (≠ I264), A310 (= A336), V316 (≠ L347), R344 (= R375), E715 (= E748), L716 (≠ A749)
- binding pterin cytosine dinucleotide: G233 (= G258), G234 (= G259), F235 (= F260), I461 (≠ H509), G462 (= G510), T463 (≠ Q511), G464 (= G512), I468 (≠ T516), G500 (= G557), S502 (= S559), Q503 (≠ A560), L504 (≠ I561), A505 (≠ M562), R638 (≠ N671), Y640 (≠ I673), N641 (= N674), Q648 (= Q681), K711 (= K744), V713 (≠ C746), G714 (= G747), E715 (= E748)
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
26% identity, 98% coverage: 10:786/795 of query aligns to 545:1268/1290 of 4uhxA
- active site: Q732 (= Q228), V767 (≠ I264), M843 (≠ V339), K847 (≠ L343), R875 (= R375), G1223 (= G747), E1224 (= E748)
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A522), R1015 (≠ D523), R1018 (≠ G526), M1019 (≠ L527), P1020 (= P528), W1079 (≠ I587)
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A522), R1015 (≠ D523), R1018 (≠ G526), M1019 (≠ L527), P1020 (= P528)
Sites not aligning to the query:
- 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
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: 540, 542, 543
8emtA Cryo-em analysis of the human aldehyde oxidase from liver (see paper)
26% identity, 98% coverage: 10:786/795 of query aligns to 504:1232/1254 of 8emtA
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 215, 216, 217, 218, 219, 221, 222, 223, 296, 297, 306, 309, 310, 312, 319
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 45, 46, 49, 69, 71, 111, 112, 114, 146, 148
4usaA Aldehyde oxidoreductase from desulfovibrio gigas (mop), soaked with trans-cinnamaldehyde (see paper)
25% identity, 99% coverage: 4:789/795 of query aligns to 170:907/907 of 4usaA
- active site: I390 (≠ P230), F425 (= F265), R501 (≠ L343), F505 (≠ L347), R533 (= R375), E869 (= E748), L870 (≠ A749)
- binding bicarbonate ion: R460 (≠ G300), A531 (= A373), F532 (≠ Y374), Y535 (≠ A377), Q539 (≠ E381)
- binding hydrocinnamic acid: I255 (≠ C86), F425 (= F265), F494 (= F335), L497 (≠ S338), Y535 (≠ A377), L626 (= L471)
- binding magnesium ion: E899 (≠ H781), E903 (≠ S785)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): T420 (≠ G259), F421 (= F260), G422 (= G261), R533 (= R375), W650 (≠ S506), H653 (= H509), G654 (= G510), Q655 (= Q511), G656 (= G512), S695 (≠ T548), G696 (≠ Y549), G697 (= G550), Q700 (≠ S553), Q701 (≠ I554), C799 (≠ I673), N800 (= N674), T804 (≠ V678), Q807 (= Q681), S865 (≠ K744), G866 (= G745), V867 (≠ C746), G868 (= G747), E869 (= E748)
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
>H281DRAFT_02182 FitnessBrowser__Burk376:H281DRAFT_02182
MNAPETHSLIGASVERKEDYRFLTGNGQYTDDILLPQQTYAVFLRSPHAHAKINSIDTTA
AKQSPGVVAIFTGADMAAENVGGLPCGWLIHSTDGKPMNEPPHPIIAHTKVRHVGDQVAL
VIADSIKAAKDAAELIEVDYDVLPAVVDTAHAADAGQPAVHDEVPDNVCYNWGHGDKAAT
DAAFAKAAHVTTLDIVNNRLVPNAIEPRAVNASYSSQDDSYTLYVANQNPHVERLLMAAF
VLSLPESKLRVIAPDVGGGFGSKIFLYAEDVALTWASKKIRRPVKWTAERSEAFLSDAHG
RDHVTKAELAMDADGKFLAMRIHTIANMGAYLSTFASSVPTILYATLLAGQYATPAIYAE
VKAVFTNTVPVDAYRGAGRPEATYVVERLVETAAREMKLDPAEIRRRNFIREFPYATPVG
LTYDTGDYETILARSLELADVKGFEARRQESERNGKRRGLGYSCYIEACGLAPSNIAGAL
GARAGLFEVGQIRVHPTGSVTVFTGSHSHGQGHETTFAQVVADRLGLPLESVEIVHGDTG
RIPFGMGTYGSRSIAVGGSAIMKALDKIETKAKKIAAHLLEAATEDIEFKDGVFRVAGTD
RTKAFAEISLAAYVPHNYPLDVLEPGLEESAFYDPSNFTYPSGAYICEVEVDPDTGVCRI
QRFTAVDDFGNVINPMIVEGQVHGGLGQGIGQAMLERCVYDNESGQLLSGSYMDYAMPHA
SDLPDFTVETAKGTPCTHNPLGVKGCGEAGAIGSPPAVINAIIDALAPLGVTDLQMPATP
HRVWSAIHAVKQAAH
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