SitesBLAST
Comparing RR42_RS02365 FitnessBrowser__Cup4G11:RR42_RS02365 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)
40% identity, 98% coverage: 10:787/793 of query aligns to 12:791/797 of 1ffvB
- active site: Q231 (= Q227), V266 (≠ I263), P343 (≠ Y343), I349 (vs. gap), R378 (= R374), C379 (≠ G375), E751 (= E747), S752 (≠ A748)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G257), G261 (= G258), F262 (= F259), G263 (= G260), A376 (= A372), R378 (= R374), C379 (≠ G375), Q516 (≠ H508), G517 (= G509), Q518 (= Q510), H520 (= H512), T523 (= T515), Y556 (= Y548), G557 (= G549), S558 (= S550), S560 (= S552), T561 (≠ L553), C674 (≠ F668), I678 (= I672), I683 (≠ V677), Q686 (= Q680), K747 (= K743), G748 (= G744), V749 (≠ C745), A750 (≠ G746), E751 (= E747)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
40% identity, 98% coverage: 10:787/793 of query aligns to 12:791/797 of 1ffuB
- active site: Q231 (= Q227), V266 (≠ I263), P343 (≠ Y343), I349 (vs. gap), R378 (= R374), C379 (≠ G375), E751 (= E747), S752 (≠ A748)
- binding cytidine-5'-diphosphate: Q518 (= Q510), H520 (= H512), T523 (= T515), S558 (= S550), S560 (= S552), T561 (≠ L553), C674 (≠ F668), T676 (≠ N670), I678 (= I672), I683 (≠ V677), K747 (= K743), G748 (= G744), V749 (≠ C745), A750 (≠ G746)
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)
40% identity, 97% coverage: 17:787/793 of query aligns to 25:797/803 of P19913
- R384 (= R374) modified: 4-hydroxyarginine
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: 10:784/793 of query aligns to 21:800/809 of P19919
- C388 (≠ G375) binding
- E763 (= E747) binding
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
39% identity, 98% coverage: 10:784/793 of query aligns to 16:795/804 of 1zxiB
- active site: Q235 (= Q227), V270 (≠ I263), P347 (≠ T340), I353 (≠ L346), R382 (= R374), C383 (≠ G375), E758 (= E747), S759 (≠ A748)
- binding copper (ii) ion: C383 (≠ G375), S384 (≠ A376), E758 (= E747)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F259), G267 (= G260), A380 (= A372), Y381 (= Y373), R382 (= R374), C383 (≠ G375), Y563 (= Y548), G564 (= G549), E758 (= E747)
- binding pterin cytosine dinucleotide: G265 (= G258), F266 (= F259), R382 (= R374), Q523 (≠ H508), G524 (= G509), Q525 (= Q510), H527 (= H512), T530 (= T515), T562 (= T547), Y563 (= Y548), S565 (= S550), S567 (= S552), T568 (≠ L553), C681 (≠ F668), I685 (= I672), I689 (= I676), I690 (≠ V677), Q693 (= Q680), K754 (= K743), G755 (= G744), V756 (≠ C745), E758 (= E747)
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
39% identity, 98% coverage: 10:784/793 of query aligns to 17:796/805 of 1n63B
- active site: Q236 (= Q227), V271 (≠ I263), P348 (≠ T340), I354 (≠ L346), R383 (= R374), C384 (≠ G375), E759 (= E747), S760 (≠ A748)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G260), A381 (= A372), R383 (= R374), C384 (≠ G375), Y564 (= Y548), G565 (= G549), E759 (= E747)
- binding pterin cytosine dinucleotide: G266 (= G258), F267 (= F259), R383 (= R374), Q524 (≠ H508), G525 (= G509), Q526 (= Q510), H528 (= H512), T531 (= T515), T563 (= T547), Y564 (= Y548), S566 (= S550), S568 (= S552), T569 (≠ L553), C682 (≠ F668), I686 (= I672), I690 (= I676), I691 (≠ V677), Q694 (= Q680), K755 (= K743), G756 (= G744), V757 (≠ C745), E759 (= E747)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
39% identity, 98% coverage: 10:784/793 of query aligns to 16:795/804 of 1n62B
- active site: Q235 (= Q227), V270 (≠ I263), P347 (≠ T340), I353 (≠ L346), R382 (= R374), C383 (≠ G375), E758 (= E747), S759 (≠ A748)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G260), V379 (vs. gap), A380 (= A372), R382 (= R374), C383 (≠ G375), F385 (≠ G377), Y563 (= Y548), G564 (= G549), E758 (= E747)
- binding pterin cytosine dinucleotide: G265 (= G258), F266 (= F259), R382 (= R374), Q523 (≠ H508), G524 (= G509), Q525 (= Q510), H527 (= H512), T530 (= T515), T562 (= T547), Y563 (= Y548), G564 (= G549), S565 (= S550), S567 (= S552), T568 (≠ L553), C681 (≠ F668), I685 (= I672), I689 (= I676), I690 (≠ V677), Q693 (= Q680), K754 (= K743), G755 (= G744), V756 (≠ C745), G757 (= G746), E758 (= E747)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
39% identity, 98% coverage: 10:784/793 of query aligns to 16:795/804 of 1n5wB
- active site: Q235 (= Q227), V270 (≠ I263), P347 (≠ T340), I353 (≠ L346), R382 (= R374), C383 (≠ G375), E758 (= E747), S759 (≠ A748)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G260), A380 (= A372), R382 (= R374), C383 (≠ G375), Y563 (= Y548), G564 (= G549), E758 (= E747)
- binding pterin cytosine dinucleotide: G265 (= G258), F266 (= F259), R382 (= R374), Q523 (≠ H508), G524 (= G509), Q525 (= Q510), H527 (= H512), T530 (= T515), T562 (= T547), Y563 (= Y548), S565 (= S550), S567 (= S552), T568 (≠ L553), C681 (≠ F668), I685 (= I672), I689 (= I676), I690 (≠ V677), Q693 (= Q680), K754 (= K743), G755 (= G744), V756 (≠ C745), E758 (= E747)
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
39% identity, 98% coverage: 10:784/793 of query aligns to 15:794/803 of 1n60B
- active site: Q234 (= Q227), V269 (≠ I263), P346 (≠ T340), I352 (≠ L346), R381 (= R374), C382 (≠ G375), E757 (= E747), S758 (≠ A748)
- binding pterin cytosine dinucleotide: G264 (= G258), F265 (= F259), R381 (= R374), Q522 (≠ H508), G523 (= G509), Q524 (= Q510), H526 (= H512), T529 (= T515), T561 (= T547), Y562 (= Y548), G563 (= G549), S564 (= S550), S566 (= S552), T567 (≠ L553), C680 (≠ F668), I684 (= I672), I688 (= I676), I689 (≠ V677), Q692 (= Q680), K753 (= K743), G754 (= G744), V755 (≠ C745), E757 (= E747)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F259), G266 (= G260), Y562 (= Y548), G563 (= G549), E757 (= E747)
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
36% identity, 98% coverage: 10:787/793 of query aligns to 14:783/786 of 1t3qB
- active site: Q224 (= Q227), A259 (≠ I263), E336 (≠ P339), V343 (≠ L346), R371 (= R374), E743 (= E747), S744 (≠ A748)
- binding pterin cytosine dinucleotide: G254 (= G258), F255 (= F259), R371 (= R374), S506 (≠ H508), G507 (= G509), Q508 (= Q510), H510 (= H512), T513 (= T515), Y545 (= Y548), S547 (= S550), G549 (≠ S552), A550 (≠ L553), C666 (≠ F668), I670 (= I672), I674 (= I676), V675 (= V677), Q678 (= Q680), K739 (= K743), G740 (= G744), M741 (≠ C745), G742 (= G746)
7dqxD Crystal structure of xanthine dehydrogenase family protein
34% identity, 98% coverage: 5:783/793 of query aligns to 1:763/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G257), S248 (≠ G258), F249 (= F259), R363 (= R374), V491 (≠ H508), G492 (= G509), Q493 (= Q510), G494 (= G511), V498 (≠ T515), S530 (≠ T547), W531 (≠ Y548), S532 (≠ G549), S533 (= S550), R534 (= R551), S535 (= S552), T536 (≠ L553), T658 (≠ I676), T659 (≠ V677), Q662 (= Q680), G725 (= G744), L726 (≠ C745), G727 (= G746), E728 (= E747)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
35% identity, 95% coverage: 10:761/793 of query aligns to 3:682/701 of 4zohA
- active site: Q186 (= Q227), I219 (= I263), V298 (≠ L342), S300 (≠ A344), M304 (≠ L346), R332 (= R374), E668 (= E747), A669 (= A748)
- binding pterin cytosine dinucleotide: G213 (= G257), A214 (≠ G258), F215 (= F259), R332 (= R374), H442 (= H508), G443 (= G509), Q444 (= Q510), D446 (≠ H512), W482 (≠ Y548), S484 (= S550), T486 (≠ S552), V487 (≠ L553), I594 (= I672), N595 (= N673), L598 (≠ I676), Q602 (= Q680), K664 (= K743), G665 (= G744), I666 (≠ C745), G667 (= G746), E668 (= E747)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
31% identity, 96% coverage: 23:782/793 of query aligns to 16:750/761 of 1rm6A
- active site: Q206 (= Q227), T241 (≠ I263), Y318 (= Y343), L322 (= L346), R350 (= R374), E718 (= E747), G719 (≠ A748)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G257), G236 (= G258), F237 (= F259), G238 (= G260), R350 (= R374), I473 (≠ H508), G474 (= G509), Q475 (= Q510), G476 (= G511), Y513 (= Y548), S514 (≠ G549), S515 (= S550), V517 (≠ S552), T518 (≠ L553), L646 (≠ I672), N647 (= N673), V651 (= V677), Q654 (= Q680), K714 (= K743), E715 (≠ G744), A716 (≠ C745), S717 (≠ G746), E718 (= E747)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
31% identity, 96% coverage: 23:782/793 of query aligns to 24:758/769 of O33819
Q8GUQ8 Xanthine dehydrogenase 1; AtXDH1; EC 1.17.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 96% coverage: 23:782/793 of query aligns to 611:1338/1361 of Q8GUQ8
- E831 (vs. gap) mutation to A: Loss of activity.
- R909 (≠ T340) mutation to A: Decreases activity 12-fold.
- E1297 (≠ S753) 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.
7orcB Human aldehyde oxidase in complex with raloxifene (see paper)
25% identity, 97% coverage: 10:782/793 of query aligns to 543:1274/1299 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)
25% identity, 97% coverage: 10:782/793 of query aligns to 580:1311/1338 of Q06278
- R802 (≠ D254) to C: decreases homodimerization but nearly no effect on kinetic parameters; dbSNP:rs41309768
- AF 806:807 (≠ GF 258:259) 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 (≠ H508) binding
- GSVV 1088:1091 (≠ GSRS 549:552) binding
- N1135 (≠ T603) 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 (= Q680) binding
- L1268 (≠ C745) binding
- G1269 (= G746) mutation to R: No effect on dimerization. Loss of oxidase activity.
- S1271 (≠ A748) to L: no effect on dimerization; no effect on oxidase activity; dbSNP:rs141786030
- H1297 (= H771) 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
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
25% identity, 97% coverage: 10:782/793 of query aligns to 545:1265/1290 of 4uhxA
- active site: Q732 (= Q227), V767 (≠ I263), M843 (≠ V338), K847 (≠ L342), R875 (= R374), G1223 (= G746), E1224 (= E747)
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A521), R1015 (≠ D522), R1018 (≠ G525), M1019 (≠ I526), P1020 (≠ A527), W1079 (≠ F593)
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A521), R1015 (≠ D522), R1018 (≠ G525), M1019 (≠ I526), P1020 (≠ A527)
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
2w54B Crystal structure of xanthine dehydrogenase from rhodobacter capsulatus in complex with bound inhibitor pterin-6-aldehyde (see paper)
27% identity, 97% coverage: 23:790/793 of query aligns to 15:757/760 of 2w54B
- active site: Q196 (= Q227), E231 (≠ F259), R309 (≠ Y343), H313 (≠ L347), R341 (= R374), G712 (= G752), E713 (≠ S753)
- binding 6-hydroxymethylpterin: E231 (≠ F259), P305 (= P339), R309 (≠ Y343), F343 (≠ A376), F442 (≠ C468), T443 (≠ G469), L444 (= L470), A512 (≠ G549), E713 (≠ S753)
- binding {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-kappaS)-3,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2-) phosphate}(hydroxy)oxo(thioxo)molybdenum: G226 (≠ D254), F227 (≠ V255), G228 (= G256), F340 (≠ Y373), R341 (= R374), M471 (≠ H508), G472 (= G509), Q473 (= Q510), A511 (≠ Y548), S513 (= S550), G515 (≠ S552), Q646 (= Q680), E713 (≠ S753)
2w3sB Crystal structure of xanthine dehydrogenase (desulfo form) from rhodobacter capsulatus in complex with xanthine (see paper)
27% identity, 97% coverage: 23:790/793 of query aligns to 15:757/760 of 2w3sB
- active site: Q196 (= Q227), E231 (≠ F259), R309 (≠ Y343), H313 (≠ L347), R341 (= R374), G712 (= G752), E713 (≠ S753)
- binding calcium ion: E171 (≠ R198), H172 (≠ L199), Y174 (≠ A203), T265 (≠ D296), G266 (≠ A297)
- binding hydroxy(dioxo)molybdenum: G228 (= G256), R341 (= R374), A511 (≠ Y548), E713 (≠ S753)
- binding xanthine: E231 (≠ F259), F343 (≠ A376), F442 (≠ C468), T443 (≠ G469), L444 (= L470), A511 (≠ Y548), A512 (≠ G549)
Query Sequence
>RR42_RS02365 FitnessBrowser__Cup4G11:RR42_RS02365
MNAPDNQHLIGASVKRKEDYRFLTGNGQYTDDIVLPQQSYGYFLRSPHAHARIVSIDKTE
ALASPGVVAIFTGDDVAADKVGGLPCGWLIHSIDGSPMKEPAHPVLAQGKARHVGDQVAL
VIAETLQQAKDAAEKIDVQYDELPAVVNTAHAASATSLVHDDVPENTSYVWGHGDRAATD
AAFAKAAHVTTLEIINNRLIPNAIEPRAVNASYTRQDDSYTVYVSNQNPHVERLLMGAFV
LGLPESRLRIIAPDVGGGFGSKIFLYAEDVALTWASKKIKRPIKWTAERSESFLTDAHGR
DHVTKAELAMDADGKFLAMRVHTTANMGAYLSTFASSVPTILYATLLAGQYATPAIYAEV
RAVFTNTAPVDAYRGAGRPEATYVVERLVEAAAREMKMDPAQIRRKNFIHDFPYATPVGL
TYDTGDYEPCLARAQELADVKGFPARREEAKQRGKLRGLGYSCYIEACGLAPSNIAGALG
ARAGLFEVGEIRVHPTGTVTVFTGSHSHGQGHETTFAQIVADRLGIALDAVEVVHGDTGR
VPFGMGTYGSRSLSVGGSAIMKALDKIEAKAKKIAAHLLEASDADIEFKNGTFSVAGTDR
SKTFGEVALTAYVPHNYPLDKLEPGLNENAFYDPTNFTYPSGAYICEVEVDPDTGESKVI
KFTAVDDFGNIINPMIVEGQVHGGIGQGLGQAMLEQCVYDDDSGQLLTGSYMDYAMPRAG
DLPDFTVETAKGTPCTHNPLGVKGCGEAGAIGSPPAFINALVDALSPLGVHDIQMPATPH
RVWQDIRLAQAPN
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