SitesBLAST
Comparing Ac3H11_3591 FitnessBrowser__acidovorax_3H11:Ac3H11_3591 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)
40% identity, 98% coverage: 12:792/795 of query aligns to 12:792/797 of 1ffvB
- active site: Q231 (= Q232), V266 (≠ I268), P343 (≠ Y348), I349 (vs. gap), R378 (= R379), C379 (≠ G380), E751 (= E751), S752 (≠ A752)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G262), G261 (= G263), F262 (= F264), G263 (= G265), A376 (= A377), R378 (= R379), C379 (≠ G380), Q516 (≠ H513), G517 (= G514), Q518 (= Q515), H520 (= H517), T523 (= T520), Y556 (= Y553), G557 (= G554), S558 (= S555), S560 (= S557), T561 (≠ I558), C674 (≠ F673), I678 (= I677), I683 (≠ V682), Q686 (= Q685), K747 (= K747), G748 (= G748), V749 (≠ C749), A750 (≠ G750), E751 (= E751)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
40% identity, 98% coverage: 12:792/795 of query aligns to 12:792/797 of 1ffuB
- active site: Q231 (= Q232), V266 (≠ I268), P343 (≠ Y348), I349 (vs. gap), R378 (= R379), C379 (≠ G380), E751 (= E751), S752 (≠ A752)
- binding cytidine-5'-diphosphate: Q518 (= Q515), H520 (= H517), T523 (= T520), S558 (= S555), S560 (= S557), T561 (≠ I558), C674 (≠ F673), T676 (= T675), I678 (= I677), I683 (≠ V682), K747 (= K747), G748 (= G748), V749 (≠ C749), A750 (≠ G750)
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: 19:792/795 of query aligns to 25:798/803 of P19913
- R384 (= R379) modified: 4-hydroxyarginine
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
39% identity, 98% coverage: 7:788/795 of query aligns to 10:794/803 of 1n60B
- active site: Q234 (= Q232), V269 (≠ I268), P346 (≠ T345), I352 (≠ L351), R381 (= R379), C382 (≠ G380), E757 (= E751), S758 (≠ A752)
- binding pterin cytosine dinucleotide: G264 (= G263), F265 (= F264), R381 (= R379), Q522 (≠ H513), G523 (= G514), Q524 (= Q515), H526 (= H517), T529 (= T520), T561 (= T552), Y562 (= Y553), G563 (= G554), S564 (= S555), S566 (= S557), T567 (≠ I558), C680 (≠ F673), I684 (= I677), I688 (= I681), I689 (≠ V682), Q692 (= Q685), K753 (= K747), G754 (= G748), V755 (≠ C749), E757 (= E751)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F264), G266 (= G265), Y562 (= Y553), G563 (= G554), E757 (= E751)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
39% identity, 98% coverage: 7:788/795 of query aligns to 11:795/804 of 1n62B
- active site: Q235 (= Q232), V270 (≠ I268), P347 (≠ T345), I353 (≠ L351), R382 (= R379), C383 (≠ G380), E758 (= E751), S759 (≠ A752)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G265), V379 (vs. gap), A380 (= A377), R382 (= R379), C383 (≠ G380), F385 (≠ G382), Y563 (= Y553), G564 (= G554), E758 (= E751)
- binding pterin cytosine dinucleotide: G265 (= G263), F266 (= F264), R382 (= R379), Q523 (≠ H513), G524 (= G514), Q525 (= Q515), H527 (= H517), T530 (= T520), T562 (= T552), Y563 (= Y553), G564 (= G554), S565 (= S555), S567 (= S557), T568 (≠ I558), C681 (≠ F673), I685 (= I677), I689 (= I681), I690 (≠ V682), Q693 (= Q685), K754 (= K747), G755 (= G748), V756 (≠ C749), G757 (= G750), E758 (= E751)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
39% identity, 98% coverage: 7:788/795 of query aligns to 11:795/804 of 1n5wB
- active site: Q235 (= Q232), V270 (≠ I268), P347 (≠ T345), I353 (≠ L351), R382 (= R379), C383 (≠ G380), E758 (= E751), S759 (≠ A752)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G265), A380 (= A377), R382 (= R379), C383 (≠ G380), Y563 (= Y553), G564 (= G554), E758 (= E751)
- binding pterin cytosine dinucleotide: G265 (= G263), F266 (= F264), R382 (= R379), Q523 (≠ H513), G524 (= G514), Q525 (= Q515), H527 (= H517), T530 (= T520), T562 (= T552), Y563 (= Y553), S565 (= S555), S567 (= S557), T568 (≠ I558), C681 (≠ F673), I685 (= I677), I689 (= I681), I690 (≠ V682), Q693 (= Q685), K754 (= K747), G755 (= G748), V756 (≠ C749), E758 (= E751)
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
39% identity, 98% coverage: 7:788/795 of query aligns to 12:796/805 of 1n63B
- active site: Q236 (= Q232), V271 (≠ I268), P348 (≠ T345), I354 (≠ L351), R383 (= R379), C384 (≠ G380), E759 (= E751), S760 (≠ A752)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G265), A381 (= A377), R383 (= R379), C384 (≠ G380), Y564 (= Y553), G565 (= G554), E759 (= E751)
- binding pterin cytosine dinucleotide: G266 (= G263), F267 (= F264), R383 (= R379), Q524 (≠ H513), G525 (= G514), Q526 (= Q515), H528 (= H517), T531 (= T520), T563 (= T552), Y564 (= Y553), S566 (= S555), S568 (= S557), T569 (≠ I558), C682 (≠ F673), I686 (= I677), I690 (= I681), I691 (≠ V682), Q694 (= Q685), K755 (= K747), G756 (= G748), V757 (≠ C749), E759 (= E751)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
39% identity, 98% coverage: 7:788/795 of query aligns to 11:795/804 of 1zxiB
- active site: Q235 (= Q232), V270 (≠ I268), P347 (≠ T345), I353 (≠ L351), R382 (= R379), C383 (≠ G380), E758 (= E751), S759 (≠ A752)
- binding copper (ii) ion: C383 (≠ G380), S384 (≠ A381), E758 (= E751)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F264), G267 (= G265), A380 (= A377), Y381 (= Y378), R382 (= R379), C383 (≠ G380), Y563 (= Y553), G564 (= G554), E758 (= E751)
- binding pterin cytosine dinucleotide: G265 (= G263), F266 (= F264), R382 (= R379), Q523 (≠ H513), G524 (= G514), Q525 (= Q515), H527 (= H517), T530 (= T520), T562 (= T552), Y563 (= Y553), S565 (= S555), S567 (= S557), T568 (≠ I558), C681 (≠ F673), I685 (= I677), I689 (= I681), I690 (≠ V682), Q693 (= Q685), K754 (= K747), G755 (= G748), V756 (≠ C749), E758 (= E751)
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: 7:788/795 of query aligns to 16:800/809 of P19919
- C388 (≠ G380) binding
- E763 (= E751) binding
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
37% identity, 99% coverage: 8:791/795 of query aligns to 10:783/786 of 1t3qB
- active site: Q224 (= Q232), A259 (≠ I268), E336 (≠ P344), V343 (≠ L351), R371 (= R379), E743 (= E751), S744 (≠ A752)
- binding pterin cytosine dinucleotide: G254 (= G263), F255 (= F264), R371 (= R379), S506 (≠ H513), G507 (= G514), Q508 (= Q515), H510 (= H517), T513 (= T520), Y545 (= Y553), S547 (= S555), G549 (≠ S557), A550 (≠ I558), C666 (≠ F673), I670 (= I677), I674 (= I681), V675 (= V682), Q678 (= Q685), K739 (= K747), G740 (= G748), M741 (≠ C749), G742 (= G750)
7dqxD Crystal structure of xanthine dehydrogenase family protein
35% identity, 93% coverage: 12:751/795 of query aligns to 6:728/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G262), S248 (≠ G263), F249 (= F264), R363 (= R379), V491 (≠ H513), G492 (= G514), Q493 (= Q515), G494 (= G516), V498 (≠ T520), S530 (≠ T552), W531 (≠ Y553), S532 (≠ G554), S533 (= S555), R534 (= R556), S535 (= S557), T536 (≠ I558), T658 (≠ I681), T659 (≠ V682), Q662 (= Q685), G725 (= G748), L726 (≠ C749), G727 (= G750), E728 (= E751)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
34% identity, 96% coverage: 11:770/795 of query aligns to 2:687/701 of 4zohA
- active site: Q186 (= Q232), I219 (= I268), V298 (≠ L347), S300 (≠ A349), M304 (≠ L351), R332 (= R379), E668 (= E751), A669 (= A752)
- binding pterin cytosine dinucleotide: G213 (= G262), A214 (≠ G263), F215 (= F264), R332 (= R379), H442 (= H513), G443 (= G514), Q444 (= Q515), D446 (≠ H517), W482 (≠ Y553), S484 (= S555), T486 (≠ S557), V487 (≠ I558), I594 (= I677), N595 (= N678), L598 (≠ I681), Q602 (= Q685), K664 (= K747), G665 (= G748), I666 (≠ C749), G667 (= G750), E668 (= E751)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
31% identity, 97% coverage: 25:795/795 of query aligns to 16:759/761 of 1rm6A
- active site: Q206 (= Q232), T241 (≠ I268), Y318 (= Y348), L322 (= L351), R350 (= R379), E718 (= E751), G719 (≠ A752)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G262), G236 (= G263), F237 (= F264), G238 (= G265), R350 (= R379), I473 (≠ H513), G474 (= G514), Q475 (= Q515), G476 (= G516), Y513 (= Y553), S514 (≠ G554), S515 (= S555), V517 (≠ S557), T518 (≠ I558), L646 (≠ I677), N647 (= N678), V651 (= V682), Q654 (= Q685), K714 (= K747), E715 (≠ G748), A716 (≠ C749), S717 (≠ G750), E718 (= E751)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
31% identity, 97% coverage: 25:795/795 of query aligns to 24:767/769 of O33819
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
26% identity, 93% coverage: 12:753/795 of query aligns to 545:1226/1290 of 4uhxA
- active site: Q732 (= Q232), V767 (≠ I268), M843 (≠ V343), K847 (≠ L347), R875 (= R379), G1223 (= G750), E1224 (= E751)
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A526), R1015 (≠ A527), R1018 (≠ G530), M1019 (≠ I531), P1020 (= P532), W1079 (≠ F598)
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: S1014 (≠ A526), R1015 (≠ A527), R1018 (≠ G530), M1019 (≠ I531), P1020 (= P532)
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, 94% coverage: 8:753/795 of query aligns to 500:1190/1254 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
7orcB Human aldehyde oxidase in complex with raloxifene (see paper)
26% identity, 93% coverage: 12:753/795 of query aligns to 543:1235/1299 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)
26% identity, 93% coverage: 12:753/795 of query aligns to 580:1272/1338 of Q06278
- R802 (≠ D259) to C: decreases homodimerization but nearly no effect on kinetic parameters; dbSNP:rs41309768
- AF 806:807 (≠ GF 263:264) binding
- R921 (= R379) 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 (≠ H513) binding
- GSVV 1088:1091 (≠ GSRS 554:557) binding
- N1135 (≠ P608) 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 (= Q685) binding
- L1268 (≠ C749) binding
- G1269 (= G750) mutation to R: No effect on dimerization. Loss of oxidase activity.
- S1271 (≠ A752) to L: no effect on dimerization; no effect on oxidase activity; dbSNP:rs141786030
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
- 1297 H → 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
2w54B Crystal structure of xanthine dehydrogenase from rhodobacter capsulatus in complex with bound inhibitor pterin-6-aldehyde (see paper)
27% identity, 98% coverage: 12:794/795 of query aligns to 2:757/760 of 2w54B
- active site: Q196 (= Q232), E231 (≠ I268), R309 (≠ Y348), H313 (≠ L352), R341 (= R379), G712 (= G756), E713 (≠ S757)
- binding 6-hydroxymethylpterin: E231 (≠ I268), P305 (= P344), R309 (≠ Y348), F343 (≠ A381), F442 (≠ C473), T443 (≠ G474), L444 (≠ I475), A512 (≠ G554), E713 (≠ S757)
- 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 (= G263), F227 (= F264), G228 (= G265), F340 (≠ Y378), R341 (= R379), M471 (≠ H513), G472 (= G514), Q473 (= Q515), A511 (≠ Y553), S513 (= S555), G515 (≠ S557), Q646 (= Q685), E713 (≠ S757)
2w3sB Crystal structure of xanthine dehydrogenase (desulfo form) from rhodobacter capsulatus in complex with xanthine (see paper)
27% identity, 98% coverage: 12:794/795 of query aligns to 2:757/760 of 2w3sB
- active site: Q196 (= Q232), E231 (≠ I268), R309 (≠ Y348), H313 (≠ L352), R341 (= R379), G712 (= G756), E713 (≠ S757)
- binding calcium ion: E171 (≠ I205), H172 (≠ P206), Y174 (≠ A208), T265 (≠ D301), G266 (≠ A302)
- binding hydroxy(dioxo)molybdenum: G228 (= G265), R341 (= R379), A511 (≠ Y553), E713 (≠ S757)
- binding xanthine: E231 (≠ I268), F343 (≠ A381), F442 (≠ C473), T443 (≠ G474), L444 (≠ I475), A511 (≠ Y553), A512 (≠ G554)
Query Sequence
>Ac3H11_3591 FitnessBrowser__acidovorax_3H11:Ac3H11_3591
MGASDFSKLPHIGESLKRKEDYRFLTGAGQYTDDVVLAAQCHAVFVRSPHAHAGINSINT
SAAKAAPGVLGVFVGADVAADNINGLPCGWLITSTNGEPMKEPPHPILAQGKVRYVGDHV
AMVVAQTLQQARDAAELVEVDYDVLPAVVNVADAAAGAVAGAALHDIAPDNHCFKWAIGD
KGAVDAAFAGAAHVTQLDLINNRLIPNAMEPRAAIGSYSRANDEYTLYVSNQNPHVERLL
MTAFVMGLPEHKVRVIAPDVGGGFGSKIYLYAEDVCLTWAAKKLNRNIKWVADRSESFLS
DAHGRDHISHAEMAMDKDGKFLAMRVHTHANLGAYLSTFASAVPTILYATLLAGQYTTPQ
VYVEVDSWFTNTAPVDAYRGAGRPEATYLLERLVTRCAWELGLSQDEIRKRNFITSFPYQ
TPVALQYDIGDYHACMTQAQQLADVAGFAARKAASEAKGFKRGIGYSSYIEACGIAPSNI
AGALGARAGLFECGEVRVHPTGSVTVFTGSHSHGQGHETTFAQVVAARLGIPVENVDIVH
GDTGRVPFGMGTYGSRSISVGGAAIMKALDKIEAKAKKIAAHLMEASDADIDFSGGEFTV
RGTDKKIPFGQVALTAYVPHNYPLDKLEPGLNETAFYDPTNFTFPAGTYICEVEIDPATG
STRVDKFTAVDDFGTIINPMIVEGQVHGGLVQGIGQAVLENCVYDRETGQLLTGSFMDYA
MPRADDFPEFKLGHVCTPCTHNPLGTKGCGEAGAIGSPPAVINAVLDALRPLGVKDFDMP
ASPHRVWEAIQSAKA
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