SitesBLAST
Comparing 3610816 FitnessBrowser__Dino:3610816 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)
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
37% identity, 98% coverage: 15:788/793 of query aligns to 14:782/786 of 1t3qB
- active site: Q224 (= Q227), A259 (≠ V262), E336 (= E339), V343 (= V343), R371 (= R374), E743 (= E749), S744 (≠ A750)
- binding pterin cytosine dinucleotide: G254 (≠ S257), F255 (≠ Y258), R371 (= R374), S506 (≠ Q509), G507 (= G510), Q508 (= Q511), H510 (≠ T513), T513 (≠ M516), Y545 (≠ W549), S547 (= S551), G549 (= G553), A550 (= A554), C666 (= C672), I670 (= I676), I674 (≠ L680), V675 (= V681), Q678 (= Q684), K739 (= K745), G740 (= G746), M741 (≠ A747), G742 (= G748)
1ffvB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava (see paper)
31% identity, 98% coverage: 15:788/793 of query aligns to 12:790/797 of 1ffvB
- active site: Q231 (= Q227), V266 (= V262), P343 (≠ E339), I349 (≠ L346), R378 (≠ T370), C379 (= C371), E751 (= E749), S752 (≠ A750)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G256), G261 (≠ S257), F262 (≠ Y258), G263 (= G259), A376 (vs. gap), R378 (≠ T370), C379 (= C371), Q516 (= Q509), G517 (= G510), Q518 (= Q511), H520 (≠ T513), T523 (≠ M516), Y556 (≠ W549), G557 (≠ A550), S558 (= S551), S560 (≠ G553), T561 (≠ A554), C674 (= C672), I678 (= I676), I683 (≠ V681), Q686 (= Q684), K747 (= K745), G748 (= G746), V749 (≠ A747), A750 (≠ G748), E751 (= E749)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
31% identity, 98% coverage: 15:788/793 of query aligns to 12:790/797 of 1ffuB
- active site: Q231 (= Q227), V266 (= V262), P343 (≠ E339), I349 (≠ L346), R378 (≠ T370), C379 (= C371), E751 (= E749), S752 (≠ A750)
- binding cytidine-5'-diphosphate: Q518 (= Q511), H520 (≠ T513), T523 (≠ M516), S558 (= S551), S560 (≠ G553), T561 (≠ A554), C674 (= C672), T676 (≠ R674), I678 (= I676), I683 (≠ V681), K747 (= K745), G748 (= G746), V749 (≠ A747), A750 (≠ G748)
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)
31% identity, 97% coverage: 21:788/793 of query aligns to 19:796/803 of P19913
- R384 (≠ T370) modified: 4-hydroxyarginine
7dqxD Crystal structure of xanthine dehydrogenase family protein
31% identity, 98% coverage: 12:785/793 of query aligns to 3:763/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G256), S248 (= S257), F249 (≠ Y258), R363 (= R374), V491 (≠ Q509), G492 (= G510), Q493 (= Q511), G494 (= G512), V498 (≠ M516), S530 (≠ T548), W531 (= W549), S532 (≠ A550), S533 (= S551), R534 (= R552), S535 (≠ G553), T536 (≠ A554), T658 (≠ L680), T659 (≠ V681), Q662 (= Q684), G725 (= G746), L726 (≠ A747), G727 (= G748), E728 (= E749)
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, 97% coverage: 15:786/793 of query aligns to 21:800/809 of P19919
- C388 (= C371) binding
- E763 (= E749) binding
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
31% identity, 97% coverage: 15:786/793 of query aligns to 17:796/805 of 1n63B
- active site: Q236 (= Q227), V271 (= V262), P348 (≠ E339), I354 (≠ L346), R383 (≠ T370), C384 (= C371), E759 (= E749), S760 (≠ A750)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G259), A381 (vs. gap), R383 (≠ T370), C384 (= C371), Y564 (≠ W549), G565 (≠ A550), E759 (= E749)
- binding pterin cytosine dinucleotide: G266 (≠ S257), F267 (≠ Y258), R383 (≠ T370), Q524 (= Q509), G525 (= G510), Q526 (= Q511), H528 (≠ T513), T531 (≠ M516), T563 (= T548), Y564 (≠ W549), S566 (= S551), S568 (≠ G553), T569 (≠ A554), C682 (= C672), I686 (= I676), I690 (≠ L680), I691 (≠ V681), Q694 (= Q684), K755 (= K745), G756 (= G746), V757 (≠ A747), E759 (= E749)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
31% identity, 97% coverage: 15:786/793 of query aligns to 16:795/804 of 1zxiB
- active site: Q235 (= Q227), V270 (= V262), P347 (≠ E339), I353 (≠ L346), R382 (≠ T370), C383 (= C371), E758 (= E749), S759 (≠ A750)
- binding copper (ii) ion: C383 (= C371), S384 (≠ Q372), E758 (= E749)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (≠ Y258), G267 (= G259), A380 (vs. gap), Y381 (vs. gap), R382 (≠ T370), C383 (= C371), Y563 (≠ W549), G564 (≠ A550), E758 (= E749)
- binding pterin cytosine dinucleotide: G265 (≠ S257), F266 (≠ Y258), R382 (≠ T370), Q523 (= Q509), G524 (= G510), Q525 (= Q511), H527 (≠ T513), T530 (≠ M516), T562 (= T548), Y563 (≠ W549), S565 (= S551), S567 (≠ G553), T568 (≠ A554), C681 (= C672), I685 (= I676), I689 (≠ L680), I690 (≠ V681), Q693 (= Q684), K754 (= K745), G755 (= G746), V756 (≠ A747), E758 (= E749)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
31% identity, 97% coverage: 15:786/793 of query aligns to 16:795/804 of 1n62B
- active site: Q235 (= Q227), V270 (= V262), P347 (≠ E339), I353 (≠ L346), R382 (≠ T370), C383 (= C371), E758 (= E749), S759 (≠ A750)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G259), V379 (vs. gap), A380 (vs. gap), R382 (≠ T370), C383 (= C371), F385 (≠ Y373), Y563 (≠ W549), G564 (≠ A550), E758 (= E749)
- binding pterin cytosine dinucleotide: G265 (≠ S257), F266 (≠ Y258), R382 (≠ T370), Q523 (= Q509), G524 (= G510), Q525 (= Q511), H527 (≠ T513), T530 (≠ M516), T562 (= T548), Y563 (≠ W549), G564 (≠ A550), S565 (= S551), S567 (≠ G553), T568 (≠ A554), C681 (= C672), I685 (= I676), I689 (≠ L680), I690 (≠ V681), Q693 (= Q684), K754 (= K745), G755 (= G746), V756 (≠ A747), G757 (= G748), E758 (= E749)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
31% identity, 97% coverage: 15:786/793 of query aligns to 16:795/804 of 1n5wB
- active site: Q235 (= Q227), V270 (= V262), P347 (≠ E339), I353 (≠ L346), R382 (≠ T370), C383 (= C371), E758 (= E749), S759 (≠ A750)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G259), A380 (vs. gap), R382 (≠ T370), C383 (= C371), Y563 (≠ W549), G564 (≠ A550), E758 (= E749)
- binding pterin cytosine dinucleotide: G265 (≠ S257), F266 (≠ Y258), R382 (≠ T370), Q523 (= Q509), G524 (= G510), Q525 (= Q511), H527 (≠ T513), T530 (≠ M516), T562 (= T548), Y563 (≠ W549), S565 (= S551), S567 (≠ G553), T568 (≠ A554), C681 (= C672), I685 (= I676), I689 (≠ L680), I690 (≠ V681), Q693 (= Q684), K754 (= K745), G755 (= G746), V756 (≠ A747), E758 (= E749)
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
31% identity, 97% coverage: 15:786/793 of query aligns to 15:794/803 of 1n60B
- active site: Q234 (= Q227), V269 (= V262), P346 (≠ E339), I352 (≠ L346), R381 (≠ T370), C382 (= C371), E757 (= E749), S758 (≠ A750)
- binding pterin cytosine dinucleotide: G264 (≠ S257), F265 (≠ Y258), R381 (≠ T370), Q522 (= Q509), G523 (= G510), Q524 (= Q511), H526 (≠ T513), T529 (≠ M516), T561 (= T548), Y562 (≠ W549), G563 (≠ A550), S564 (= S551), S566 (≠ G553), T567 (≠ A554), C680 (= C672), I684 (= I676), I688 (≠ L680), I689 (≠ V681), Q692 (= Q684), K753 (= K745), G754 (= G746), V755 (≠ A747), E757 (= E749)
- binding mo(vi)(=o)(oh)2 cluster: F265 (≠ Y258), G266 (= G259), Y562 (≠ W549), G563 (≠ A550), E757 (= E749)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
31% identity, 97% coverage: 14:785/793 of query aligns to 2:701/701 of 4zohA
- active site: Q186 (= Q227), I219 (≠ V262), V298 (= V343), S300 (vs. gap), M304 (≠ L346), R332 (= R374), E668 (= E749), A669 (= A750)
- binding pterin cytosine dinucleotide: G213 (= G256), A214 (≠ S257), F215 (≠ Y258), R332 (= R374), H442 (≠ Q509), G443 (= G510), Q444 (= Q511), D446 (≠ T513), W482 (= W549), S484 (= S551), T486 (≠ G553), V487 (≠ A554), I594 (= I676), N595 (= N677), L598 (= L680), Q602 (= Q684), K664 (= K745), G665 (= G746), I666 (≠ A747), G667 (= G748), E668 (= E749)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
30% identity, 97% coverage: 15:784/793 of query aligns to 3:750/761 of 1rm6A
- active site: Q206 (= Q227), T241 (≠ V262), Y318 (≠ E339), L322 (≠ V343), R350 (= R374), E718 (= E749), G719 (≠ A750)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G256), G236 (≠ S257), F237 (≠ Y258), G238 (= G259), R350 (= R374), I473 (≠ Q509), G474 (= G510), Q475 (= Q511), G476 (= G512), Y513 (≠ W549), S514 (≠ A550), S515 (= S551), V517 (≠ G553), T518 (≠ A554), L646 (≠ I676), N647 (= N677), V651 (= V681), Q654 (= Q684), K714 (= K745), E715 (≠ G746), A716 (= A747), S717 (≠ G748), E718 (= E749)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
30% identity, 98% coverage: 7:784/793 of query aligns to 2:758/769 of O33819
7orcB Human aldehyde oxidase in complex with raloxifene (see paper)
27% identity, 99% coverage: 2:784/793 of query aligns to 529:1274/1299 of 7orcB
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 43, 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 310, 318, 319, 322, 323, 326, 328, 331, 332, 376, 403
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 111, 112, 114, 146, 148
- binding raloxifene: 417, 418, 419, 449, 451, 506, 507
Q06278 Aldehyde oxidase; Aldehyde oxidase 1; Azaheterocycle hydroxylase; EC 1.2.3.1; EC 1.17.3.- from Homo sapiens (Human) (see 3 papers)
27% identity, 98% coverage: 4:784/793 of query aligns to 569:1311/1338 of Q06278
- R802 (≠ D253) to C: decreases homodimerization but nearly no effect on kinetic parameters; dbSNP:rs41309768
- AF 806:807 (≠ SY 257:258) binding
- R921 (= R374) to H: increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM; dbSNP:rs56199635
- M1047 (≠ Q509) binding
- GSVV 1088:1091 (≠ ASRG 550:553) binding
- N1135 (≠ P605) to S: increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate; dbSNP:rs55754655
- Q1203 (= Q684) binding
- L1268 (≠ A747) binding
- G1269 (= G748) mutation to R: No effect on dimerization. Loss of oxidase activity.
- S1271 (≠ A750) to L: no effect on dimerization; no effect on oxidase activity; dbSNP:rs141786030
- H1297 (≠ G771) to R: increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate; dbSNP:rs3731722
Sites not aligning to the query:
- 44 binding ; C→W: Disrupts protein stability.
- 49 binding
- 52 binding
- 74 binding
- 113 binding
- 114 binding
- 117 binding
- 149 binding
- 151 binding ; binding
- 264:271 binding
- 345 binding
- 354 binding
- 358 binding
- 367 binding
- 411 binding
8emtA Cryo-em analysis of the human aldehyde oxidase from liver (see paper)
27% identity, 97% coverage: 15:784/793 of query aligns to 504:1229/1254 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
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
27% identity, 98% coverage: 4:784/793 of query aligns to 534:1265/1290 of 4uhxA
- active site: Q732 (= Q227), V767 (= V262), M843 (≠ G340), K847 (≠ V344), R875 (= R374), G1223 (= G748), E1224 (= E749)
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: H540 (≠ R10), E542 (≠ N12), D543 (≠ S13), S1014 (≠ A522), R1015 (≠ E523), R1018 (≠ G526), M1019 (≠ V527), P1020 (= P528), W1079 (≠ A597)
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: H540 (≠ R10), E542 (≠ N12), D543 (≠ S13), S1014 (≠ A522), R1015 (≠ E523), R1018 (≠ G526), M1019 (≠ V527), 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
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
27% identity, 93% coverage: 49:785/793 of query aligns to 41:748/748 of 5y6qC
- active site: Q204 (= Q227), P239 (≠ V262), A310 (≠ P333), V316 (≠ L346), R344 (= R374), E715 (= E749), L716 (≠ A750)
- binding pterin cytosine dinucleotide: G233 (= G256), G234 (≠ S257), F235 (≠ Y258), I461 (≠ Q509), G462 (= G510), T463 (≠ Q511), G464 (= G512), I468 (≠ M516), G500 (≠ W549), S502 (= S551), Q503 (≠ R552), L504 (≠ G553), A505 (= A554), R638 (= R674), Y640 (≠ I676), N641 (= N677), Q648 (= Q684), K711 (= K745), V713 (≠ A747), G714 (= G748), E715 (= E749)
3b9jC Structure of xanthine oxidase with 2-hydroxy-6-methylpurine (see paper)
27% identity, 97% coverage: 15:787/793 of query aligns to 3:738/758 of 3b9jC
- active site: Q197 (= Q227), E232 (vs. gap), R310 (= R334), H314 (≠ I338), R342 (= R374), G690 (= G748), E691 (= E749)
- binding 6-methyl-3,9-dihydro-2H-purin-2-one: E232 (vs. gap), R310 (= R334), F344 (≠ V376), F439 (vs. gap), T440 (≠ G481), A509 (= A550), E691 (= E749)
- binding calcium ion: R269 (≠ D300), H270 (= H301)
Query Sequence
>3610816 FitnessBrowser__Dino:3610816
MTIQFGNPDRPNSYIGKTVPRPNAAKLVQGRGQYVDDITLPRMVHVAFVRSPFAHAQITG
IDAAEALATKGVLRVFTGADLAEVCTPWVAVLAHLKGLKSPPEHPIAIDRAVWVGEPVAA
VVATSRAAAEEGAALVEVDYDPLPAVTDTMTALDADTPVIHPDLGDNLAFRRLHEEGDVD
AAKAAAHKVVTARFRTARHTGVTLEPRSILVDWNPAEGQMTAYHATQAPHMMQSVLAKHL
DIPESRVRVICGDVGGSYGIKVHVYPDEVATAAIAKVMGRPVKFIADRLESFTTDIHARD
HEIEASIAVDADGKILAIDVNDWTGIGPYSVYPRTSAIEGNQVVNLCGGPYDFANYRART
SVVFQNKTPTCQYRAVGHPIAVAITEGLVDMAAAELGMDPVEIRRRNMYADDAYPVTSPA
KMKFEGLSHHASMDKLMAMMDYDALRADQAEARKAGKLRGLGIASFIELTNPSPFMYGIG
GARISAQDGCTVRMDPDGSVVALSGVTEQGQGTEAMLSQVVAEGVGVPPSQVRVITGDTQ
VTPYGGGTWASRGAGIGGEAALQAAKALRDSILQVAAAMLQAAPDTLDIRDGQVVDAATG
AERMPLAELGRIVYFRGDTLPKDLPRELVQTRHFITMDYPFAFTNGVQASYLEVDPETGV
VTLLKHWCVEDCGRVINPQLVDEQIRGGIVQGLGGALYEEIHYDADGQLLNGSMADYLVP
MAAEMPDMQIAHVETPTGESELGAKGAGEAGTAGAPAAVMNAINDALRPLGAQVTEMPFT
PERILRAMGKIEG
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