SitesBLAST
Comparing SMc03102 FitnessBrowser__Smeli:SMc03102 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)
38% identity, 99% coverage: 1:774/781 of query aligns to 7:787/797 of 1ffvB
- active site: Q231 (= Q224), V266 (≠ I260), P343 (≠ Y340), I349 (vs. gap), R378 (= R371), C379 (≠ G372), E751 (= E741), S752 (≠ A742)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G254), G261 (= G255), F262 (= F256), G263 (= G257), A376 (= A369), R378 (= R371), C379 (≠ G372), Q516 (≠ H505), G517 (= G506), Q518 (= Q507), H520 (= H509), T523 (= T512), Y556 (= Y545), G557 (= G546), S558 (= S547), S560 (= S549), T561 (≠ G550), C674 (≠ F664), I678 (= I668), I683 (≠ V673), Q686 (= Q676), K747 (= K737), G748 (= G738), V749 (≠ C739), A750 (≠ G740), E751 (= E741)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
38% identity, 99% coverage: 1:774/781 of query aligns to 7:787/797 of 1ffuB
- active site: Q231 (= Q224), V266 (≠ I260), P343 (≠ Y340), I349 (vs. gap), R378 (= R371), C379 (≠ G372), E751 (= E741), S752 (≠ A742)
- binding cytidine-5'-diphosphate: Q518 (= Q507), H520 (= H509), T523 (= T512), S558 (= S547), S560 (= S549), T561 (≠ G550), C674 (≠ F664), T676 (≠ N666), I678 (= I668), I683 (≠ V673), K747 (= K737), G748 (= G738), V749 (≠ C739), A750 (≠ G740)
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: 1:774/781 of query aligns to 13:793/803 of P19913
- R384 (= R371) modified: 4-hydroxyarginine
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
37% identity, 99% coverage: 3:774/781 of query aligns to 14:795/805 of 1n63B
- active site: Q236 (= Q224), V271 (≠ I260), P348 (≠ T337), I354 (≠ L343), R383 (= R371), C384 (≠ G372), E759 (= E741), S760 (≠ A742)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G257), A381 (= A369), R383 (= R371), C384 (≠ G372), Y564 (= Y545), G565 (= G546), E759 (= E741)
- binding pterin cytosine dinucleotide: G266 (= G255), F267 (= F256), R383 (= R371), Q524 (≠ H505), G525 (= G506), Q526 (= Q507), H528 (= H509), T531 (= T512), T563 (= T544), Y564 (= Y545), S566 (= S547), S568 (= S549), T569 (≠ G550), C682 (≠ F664), I686 (= I668), I690 (= I672), I691 (≠ V673), Q694 (= Q676), K755 (= K737), G756 (= G738), V757 (≠ C739), E759 (= E741)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
37% identity, 99% coverage: 3:774/781 of query aligns to 13:794/804 of 1n62B
- active site: Q235 (= Q224), V270 (≠ I260), P347 (≠ T337), I353 (≠ L343), R382 (= R371), C383 (≠ G372), E758 (= E741), S759 (≠ A742)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G257), V379 (vs. gap), A380 (= A369), R382 (= R371), C383 (≠ G372), F385 (≠ G374), Y563 (= Y545), G564 (= G546), E758 (= E741)
- binding pterin cytosine dinucleotide: G265 (= G255), F266 (= F256), R382 (= R371), Q523 (≠ H505), G524 (= G506), Q525 (= Q507), H527 (= H509), T530 (= T512), T562 (= T544), Y563 (= Y545), G564 (= G546), S565 (= S547), S567 (= S549), T568 (≠ G550), C681 (≠ F664), I685 (= I668), I689 (= I672), I690 (≠ V673), Q693 (= Q676), K754 (= K737), G755 (= G738), V756 (≠ C739), G757 (= G740), E758 (= E741)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
37% identity, 99% coverage: 3:774/781 of query aligns to 13:794/804 of 1n5wB
- active site: Q235 (= Q224), V270 (≠ I260), P347 (≠ T337), I353 (≠ L343), R382 (= R371), C383 (≠ G372), E758 (= E741), S759 (≠ A742)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G257), A380 (= A369), R382 (= R371), C383 (≠ G372), Y563 (= Y545), G564 (= G546), E758 (= E741)
- binding pterin cytosine dinucleotide: G265 (= G255), F266 (= F256), R382 (= R371), Q523 (≠ H505), G524 (= G506), Q525 (= Q507), H527 (= H509), T530 (= T512), T562 (= T544), Y563 (= Y545), S565 (= S547), S567 (= S549), T568 (≠ G550), C681 (≠ F664), I685 (= I668), I689 (= I672), I690 (≠ V673), Q693 (= Q676), K754 (= K737), G755 (= G738), V756 (≠ C739), E758 (= E741)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
37% identity, 99% coverage: 3:774/781 of query aligns to 13:794/804 of 1zxiB
- active site: Q235 (= Q224), V270 (≠ I260), P347 (≠ T337), I353 (≠ L343), R382 (= R371), C383 (≠ G372), E758 (= E741), S759 (≠ A742)
- binding copper (ii) ion: C383 (≠ G372), S384 (≠ A373), E758 (= E741)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F256), G267 (= G257), A380 (= A369), Y381 (= Y370), R382 (= R371), C383 (≠ G372), Y563 (= Y545), G564 (= G546), E758 (= E741)
- binding pterin cytosine dinucleotide: G265 (= G255), F266 (= F256), R382 (= R371), Q523 (≠ H505), G524 (= G506), Q525 (= Q507), H527 (= H509), T530 (= T512), T562 (= T544), Y563 (= Y545), S565 (= S547), S567 (= S549), T568 (≠ G550), C681 (≠ F664), I685 (= I668), I689 (= I672), I690 (≠ V673), Q693 (= Q676), K754 (= K737), G755 (= G738), V756 (≠ C739), E758 (= E741)
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
37% identity, 99% coverage: 3:774/781 of query aligns to 12:793/803 of 1n60B
- active site: Q234 (= Q224), V269 (≠ I260), P346 (≠ T337), I352 (≠ L343), R381 (= R371), C382 (≠ G372), E757 (= E741), S758 (≠ A742)
- binding pterin cytosine dinucleotide: G264 (= G255), F265 (= F256), R381 (= R371), Q522 (≠ H505), G523 (= G506), Q524 (= Q507), H526 (= H509), T529 (= T512), T561 (= T544), Y562 (= Y545), G563 (= G546), S564 (= S547), S566 (= S549), T567 (≠ G550), C680 (≠ F664), I684 (= I668), I688 (= I672), I689 (≠ V673), Q692 (= Q676), K753 (= K737), G754 (= G738), V755 (≠ C739), E757 (= E741)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F256), G266 (= G257), Y562 (= Y545), G563 (= G546), E757 (= E741)
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: 3:774/781 of query aligns to 18:799/809 of P19919
- C388 (≠ G372) binding
- E763 (= E741) binding
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
37% identity, 99% coverage: 4:778/781 of query aligns to 12:783/786 of 1t3qB
- active site: Q224 (= Q224), A259 (≠ I260), E336 (≠ P336), V343 (≠ L343), R371 (= R371), E743 (= E741), S744 (≠ A742)
- binding pterin cytosine dinucleotide: G254 (= G255), F255 (= F256), R371 (= R371), S506 (≠ H505), G507 (= G506), Q508 (= Q507), H510 (= H509), T513 (= T512), Y545 (= Y545), S547 (= S547), G549 (≠ S549), A550 (≠ G550), C666 (≠ F664), I670 (= I668), I674 (= I672), V675 (= V673), Q678 (= Q676), K739 (= K737), G740 (= G738), M741 (≠ C739), G742 (= G740)
7dqxD Crystal structure of xanthine dehydrogenase family protein
35% identity, 94% coverage: 6:741/781 of query aligns to 6:728/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G254), S248 (≠ G255), F249 (= F256), R363 (= R371), V491 (≠ H505), G492 (= G506), Q493 (= Q507), G494 (= G508), V498 (≠ T512), S530 (≠ T544), W531 (≠ Y545), S532 (≠ G546), S533 (= S547), R534 (= R548), S535 (= S549), T536 (≠ G550), T658 (≠ I672), T659 (≠ V673), Q662 (= Q676), G725 (= G738), L726 (≠ C739), G727 (= G740), E728 (= E741)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
33% identity, 98% coverage: 6:767/781 of query aligns to 3:694/701 of 4zohA
- active site: Q186 (= Q224), I219 (= I260), V298 (≠ L339), S300 (≠ A341), M304 (≠ L343), R332 (= R371), E668 (= E741), A669 (= A742)
- binding pterin cytosine dinucleotide: G213 (= G254), A214 (≠ G255), F215 (= F256), R332 (= R371), H442 (= H505), G443 (= G506), Q444 (= Q507), D446 (≠ H509), W482 (≠ Y545), S484 (= S547), T486 (≠ S549), V487 (≠ G550), I594 (= I668), N595 (= N669), L598 (≠ I672), Q602 (= Q676), K664 (= K737), G665 (= G738), I666 (≠ C739), G667 (= G740), E668 (= E741)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
29% identity, 98% coverage: 6:773/781 of query aligns to 3:750/761 of 1rm6A
- active site: Q206 (= Q224), T241 (≠ I260), Y318 (= Y340), L322 (= L343), R350 (= R371), E718 (= E741), G719 (≠ A742)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G254), G236 (= G255), F237 (= F256), G238 (= G257), R350 (= R371), I473 (≠ H505), G474 (= G506), Q475 (= Q507), G476 (= G508), Y513 (= Y545), S514 (≠ G546), S515 (= S547), V517 (≠ S549), T518 (≠ G550), L646 (≠ I668), N647 (= N669), V651 (= V673), Q654 (= Q676), K714 (= K737), E715 (≠ G738), A716 (≠ C739), S717 (≠ G740), E718 (= E741)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
29% identity, 98% coverage: 6:773/781 of query aligns to 11:758/769 of O33819
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
27% identity, 97% coverage: 20:776/781 of query aligns to 559:1268/1290 of 4uhxA
- active site: Q732 (= Q224), V767 (≠ I260), M843 (≠ L339), K847 (≠ L343), R875 (= R371), G1223 (= G740), E1224 (= E741)
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A518), R1015 (≠ E519), R1018 (≠ G522), M1019 (≠ V523), P1020 (= P524), W1079 (≠ L590)
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A518), R1015 (≠ E519), R1018 (≠ G522), M1019 (≠ V523), P1020 (= P524)
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)
27% identity, 99% coverage: 4:776/781 of query aligns to 502:1232/1254 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
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, 97% coverage: 20:777/781 of query aligns to 594:1315/1338 of Q06278
- R802 (≠ D251) to C: decreases homodimerization but nearly no effect on kinetic parameters; dbSNP:rs41309768
- AF 806:807 (≠ GF 255:256) binding
- R921 (= R371) 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 (≠ H505) binding
- GSVV 1088:1091 (≠ GSRS 546:549) binding
- N1135 (≠ P600) 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 (= Q676) binding
- L1268 (≠ C739) binding
- G1269 (= G740) mutation to R: No effect on dimerization. Loss of oxidase activity.
- S1271 (≠ A742) to L: no effect on dimerization; no effect on oxidase activity; dbSNP:rs141786030
- H1297 (vs. gap) 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
7orcB Human aldehyde oxidase in complex with raloxifene (see paper)
27% identity, 97% coverage: 20:776/781 of query aligns to 557:1277/1299 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
3b9jC Structure of xanthine oxidase with 2-hydroxy-6-methylpurine (see paper)
26% identity, 97% coverage: 20:773/781 of query aligns to 17:735/758 of 3b9jC
- active site: Q197 (= Q224), E232 (vs. gap), R310 (≠ T337), H314 (≠ A341), R342 (= R371), G690 (= G746), E691 (≠ S747)
- binding 6-methyl-3,9-dihydro-2H-purin-2-one: E232 (vs. gap), R310 (≠ T337), F344 (≠ A373), F439 (≠ A471), T440 (≠ A472), A509 (≠ G546), E691 (≠ S747)
- binding calcium ion: R269 (≠ G296), H270 (≠ R297)
3sr6C Crystal structure of reduced bovine xanthine oxidase in complex with arsenite (see paper)
26% identity, 97% coverage: 20:773/781 of query aligns to 17:735/745 of 3sr6C
- active site: Q197 (= Q224), E232 (vs. gap), R310 (≠ T337), H314 (≠ A341), R342 (= R371), G690 (= G746), E691 (≠ S747)
- binding [arsenothionito(2-)-kappa~2~O,S](oxo)molybdenum: G229 (= G257), F344 (≠ A373), A508 (≠ Y545), A509 (≠ G546), E691 (≠ S747)
Query Sequence
>SMc03102 FitnessBrowser__Smeli:SMc03102
MGVEGIGARVARKEDKRFLTGKGRYTDDMVVPGMKYAVFVRSPHAHATIRSIDATSAKSM
PGVIDVLDGKQLLADGIGNLICGWMIHSKDGSPMRMGAWRPLAHETVRYVGDAVAIVVAD
SVAQARDAAEAVVVDYETLPVVTETLQALGEGEPQIHPEAPGNLIFDWELGDAGAADQAI
AAAAHVTELKIINNRLSPNAMEPRATLGIYDAGDDHFTCYTTSQNPHLARLVMSAFYNVA
PENKLRVIAPDVGGGFGSKIFIYPEEIVCLWASKRTGVPVKWTADRTEAFLTDAHGRDHV
STVKMAFDSSNRITALKVDTIANLGAYMSLFSSCVPTYLYATLLSGQYAIPAIHANVRTV
YTNTAPVDAYRGAGRPEATYLLERTIETAARELGISPAELRRINFIRTFPHQTPVIMNYD
AGDYEASLRGAMEAADWDGFAARKAEAERRGMKRGIGMSCYIEACGLAPSAAVGSLGAGV
GLWESAEVRVNAVGTIEVMTGSHSHGQGHETTFAQVVAERFGVPIDSVNIVHGDTDKVQM
GMGTYGSRSGAVGMSAVFKALDKVEAKAKRIAAHMMEADESDIVIEDGALKVAGTDRSVP
WSQVALASYTAHNLPPGMEPGLKEGAFYDPSNFTFPAGCYICEVEVDPETGRTKIVQFVA
ADDFGNIINPLIVEGQVHGGLAQGIGQALLEGVHYDQSGQLLTASYMDYAMPRADDLPSF
TVTTSNTPCPSNPLGVKGCGEAGAIGSPPALINAITDAIGTNELTMPATPQKVWVAVHSA
H
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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