SitesBLAST
Comparing 3607804 FitnessBrowser__Dino:3607804 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)
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)
71% identity, 99% coverage: 7:805/806 of query aligns to 9:808/809 of P19919
- C388 (= C385) binding
- E763 (= E760) binding
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
71% identity, 99% coverage: 7:805/806 of query aligns to 5:804/805 of 1n63B
- active site: Q236 (= Q237), V271 (= V272), P348 (= P349), I354 (= I355), R383 (= R384), C384 (= C385), E759 (= E760), S760 (= S761)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G269), A381 (= A382), R383 (= R384), C384 (= C385), Y564 (= Y565), G565 (= G566), E759 (= E760)
- binding pterin cytosine dinucleotide: G266 (= G267), F267 (= F268), R383 (= R384), Q524 (= Q525), G525 (= G526), Q526 (= Q527), H528 (= H529), T531 (= T532), T563 (= T564), Y564 (= Y565), S566 (= S567), S568 (= S569), T569 (= T570), C682 (= C683), I686 (= I687), I690 (≠ V691), I691 (= I692), Q694 (= Q695), K755 (= K756), G756 (= G757), V757 (= V758), E759 (= E760)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
71% identity, 99% coverage: 7:805/806 of query aligns to 4:803/804 of 1n62B
- active site: Q235 (= Q237), V270 (= V272), P347 (= P349), I353 (= I355), R382 (= R384), C383 (= C385), E758 (= E760), S759 (= S761)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G269), V379 (= V381), A380 (= A382), R382 (= R384), C383 (= C385), F385 (= F387), Y563 (= Y565), G564 (= G566), E758 (= E760)
- binding pterin cytosine dinucleotide: G265 (= G267), F266 (= F268), R382 (= R384), Q523 (= Q525), G524 (= G526), Q525 (= Q527), H527 (= H529), T530 (= T532), T562 (= T564), Y563 (= Y565), G564 (= G566), S565 (= S567), S567 (= S569), T568 (= T570), C681 (= C683), I685 (= I687), I689 (≠ V691), I690 (= I692), Q693 (= Q695), K754 (= K756), G755 (= G757), V756 (= V758), G757 (= G759), E758 (= E760)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
71% identity, 99% coverage: 7:805/806 of query aligns to 4:803/804 of 1n5wB
- active site: Q235 (= Q237), V270 (= V272), P347 (= P349), I353 (= I355), R382 (= R384), C383 (= C385), E758 (= E760), S759 (= S761)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G269), A380 (= A382), R382 (= R384), C383 (= C385), Y563 (= Y565), G564 (= G566), E758 (= E760)
- binding pterin cytosine dinucleotide: G265 (= G267), F266 (= F268), R382 (= R384), Q523 (= Q525), G524 (= G526), Q525 (= Q527), H527 (= H529), T530 (= T532), T562 (= T564), Y563 (= Y565), S565 (= S567), S567 (= S569), T568 (= T570), C681 (= C683), I685 (= I687), I689 (≠ V691), I690 (= I692), Q693 (= Q695), K754 (= K756), G755 (= G757), V756 (= V758), E758 (= E760)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
71% identity, 99% coverage: 7:805/806 of query aligns to 4:803/804 of 1zxiB
- active site: Q235 (= Q237), V270 (= V272), P347 (= P349), I353 (= I355), R382 (= R384), C383 (= C385), E758 (= E760), S759 (= S761)
- binding copper (ii) ion: C383 (= C385), S384 (= S386), E758 (= E760)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F268), G267 (= G269), A380 (= A382), Y381 (= Y383), R382 (= R384), C383 (= C385), Y563 (= Y565), G564 (= G566), E758 (= E760)
- binding pterin cytosine dinucleotide: G265 (= G267), F266 (= F268), R382 (= R384), Q523 (= Q525), G524 (= G526), Q525 (= Q527), H527 (= H529), T530 (= T532), T562 (= T564), Y563 (= Y565), S565 (= S567), S567 (= S569), T568 (= T570), C681 (= C683), I685 (= I687), I689 (≠ V691), I690 (= I692), Q693 (= Q695), K754 (= K756), G755 (= G757), V756 (= V758), E758 (= E760)
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
71% identity, 99% coverage: 7:805/806 of query aligns to 3:802/803 of 1n60B
- active site: Q234 (= Q237), V269 (= V272), P346 (= P349), I352 (= I355), R381 (= R384), C382 (= C385), E757 (= E760), S758 (= S761)
- binding pterin cytosine dinucleotide: G264 (= G267), F265 (= F268), R381 (= R384), Q522 (= Q525), G523 (= G526), Q524 (= Q527), H526 (= H529), T529 (= T532), T561 (= T564), Y562 (= Y565), G563 (= G566), S564 (= S567), S566 (= S569), T567 (= T570), C680 (= C683), I684 (= I687), I688 (≠ V691), I689 (= I692), Q692 (= Q695), K753 (= K756), G754 (= G757), V755 (= V758), E757 (= E760)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F268), G266 (= G269), Y562 (= Y565), G563 (= G566), E757 (= E760)
1ffvB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava (see paper)
68% identity, 99% coverage: 10:804/806 of query aligns to 3:795/797 of 1ffvB
- active site: Q231 (= Q237), V266 (= V272), P343 (= P349), I349 (= I355), R378 (= R384), C379 (= C385), E751 (= E760), S752 (= S761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G266), G261 (= G267), F262 (= F268), G263 (= G269), A376 (= A382), R378 (= R384), C379 (= C385), Q516 (= Q525), G517 (= G526), Q518 (= Q527), H520 (= H529), T523 (= T532), Y556 (= Y565), G557 (= G566), S558 (= S567), S560 (= S569), T561 (= T570), C674 (= C683), I678 (= I687), I683 (= I692), Q686 (= Q695), K747 (= K756), G748 (= G757), V749 (= V758), A750 (≠ G759), E751 (= E760)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
68% identity, 99% coverage: 10:804/806 of query aligns to 3:795/797 of 1ffuB
- active site: Q231 (= Q237), V266 (= V272), P343 (= P349), I349 (= I355), R378 (= R384), C379 (= C385), E751 (= E760), S752 (= S761)
- binding cytidine-5'-diphosphate: Q518 (= Q527), H520 (= H529), T523 (= T532), S558 (= S567), S560 (= S569), T561 (= T570), C674 (= C683), T676 (= T685), I678 (= I687), I683 (= I692), K747 (= K756), G748 (= G757), V749 (= V758), A750 (≠ G759)
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)
67% identity, 99% coverage: 4:804/806 of query aligns to 1:801/803 of P19913
- R384 (= R384) modified: 4-hydroxyarginine
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
35% identity, 93% coverage: 15:761/806 of query aligns to 10:744/786 of 1t3qB
- active site: Q224 (= Q237), A259 (≠ V272), E336 (≠ P349), V343 (≠ I355), R371 (= R384), E743 (= E760), S744 (= S761)
- binding pterin cytosine dinucleotide: G254 (= G267), F255 (= F268), R371 (= R384), S506 (≠ Q525), G507 (= G526), Q508 (= Q527), H510 (= H529), T513 (= T532), Y545 (= Y565), S547 (= S567), G549 (≠ S569), A550 (≠ T570), C666 (= C683), I670 (= I687), I674 (≠ V691), V675 (≠ I692), Q678 (= Q695), K739 (= K756), G740 (= G757), M741 (≠ V758), G742 (= G759)
7dqxD Crystal structure of xanthine dehydrogenase family protein
34% identity, 92% coverage: 19:760/806 of query aligns to 6:728/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G266), S248 (≠ G267), F249 (= F268), R363 (= R384), V491 (≠ Q525), G492 (= G526), Q493 (= Q527), G494 (= G528), V498 (≠ T532), S530 (≠ T564), W531 (≠ Y565), S532 (≠ G566), S533 (= S567), R534 (= R568), S535 (= S569), T536 (= T570), T658 (≠ V691), T659 (≠ I692), Q662 (= Q695), G725 (= G757), L726 (≠ V758), G727 (= G759), E728 (= E760)
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
31% identity, 96% coverage: 19:789/806 of query aligns to 3:694/701 of 4zohA
- active site: Q186 (= Q237), I219 (≠ V272), V298 (≠ P349), S300 (≠ G351), M304 (≠ I355), R332 (= R384), E668 (= E760), A669 (≠ S761)
- binding pterin cytosine dinucleotide: G213 (= G266), A214 (≠ G267), F215 (= F268), R332 (= R384), H442 (≠ Q525), G443 (= G526), Q444 (= Q527), D446 (≠ H529), W482 (≠ Y565), S484 (= S567), T486 (≠ S569), V487 (≠ T570), I594 (= I687), N595 (= N688), L598 (≠ V691), Q602 (= Q695), K664 (= K756), G665 (= G757), I666 (≠ V758), G667 (= G759), E668 (= E760)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
28% identity, 95% coverage: 34:795/806 of query aligns to 26:758/769 of O33819
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
27% identity, 95% coverage: 34:795/806 of query aligns to 18:750/761 of 1rm6A
- active site: Q206 (= Q237), T241 (≠ V272), Y318 (≠ P349), L322 (≠ I355), R350 (= R384), E718 (= E760), G719 (≠ S761)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G266), G236 (= G267), F237 (= F268), G238 (= G269), R350 (= R384), I473 (≠ Q525), G474 (= G526), Q475 (= Q527), G476 (= G528), Y513 (= Y565), S514 (≠ G566), S515 (= S567), V517 (≠ S569), T518 (= T570), L646 (≠ I687), N647 (= N688), V651 (≠ I692), Q654 (= Q695), K714 (= K756), E715 (≠ G757), A716 (≠ V758), S717 (≠ G759), E718 (= E760)
Q7G9P4 Abscisic-aldehyde oxidase; Aldehyde oxidase 3; AO-3; AtAO-3; AtAO4; Indole-3-acetaldehyde oxidase; IAA oxidase; EC 1.2.3.14; EC 1.2.3.7 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 95% coverage: 15:780/806 of query aligns to 561:1279/1332 of Q7G9P4
- LQRPVK 821:826 (≠ TGKPVK 288:293) mutation to WDLDQ: In aao3-3; wilty phenotype in rosette leaves, reduced ABA levels, reduced dormancy, abnormal water loss and abnormal response to water deficit.
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
23% identity, 93% coverage: 34:780/806 of query aligns to 561:1253/1291 of 2e3tA
- active site: Q740 (= Q237), E775 (≠ V272), R853 (≠ A350), H857 (= H354), R885 (= R384), G1233 (= G759), E1234 (= E760)
- binding bicarbonate ion: R812 (≠ A308), H813 (≠ R309), I850 (≠ K347), T882 (≠ V381), A883 (= A382), F887 (= F387), G888 (≠ R388), Q891 (≠ E391)
- binding calcium ion: E713 (≠ H210), H714 (≠ P211), Y716 (≠ P213), T809 (= T305), G810 (≠ A306), G840 (≠ H336), T843 (≠ F339), E844 (≠ D340), S847 (≠ A343), S880 (≠ G379), N881 (≠ G380)
- binding fe2/s2 (inorganic) cluster: L717 (= L214)
- binding uric acid: E775 (≠ V272), R853 (≠ A350), F887 (= F387), F982 (≠ K493), T983 (≠ N494), A1051 (= A573), A1052 (≠ G574), E1234 (= E760)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 318, 319, 322, 323, 325, 326, 331, 332, 375, 376
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 113, 145, 147
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
23% identity, 93% coverage: 34:780/806 of query aligns to 559:1251/1291 of 6a7xB
- active site: Q738 (= Q237), E773 (≠ V272), R851 (≠ A350), H855 (= H354), R883 (= R384), G1231 (= G759), E1232 (= E760)
- binding bicarbonate ion: R810 (≠ A308), H811 (≠ R309), T880 (≠ V381), A881 (= A382), F885 (= F387), G886 (≠ R388), Q889 (≠ E391)
- binding fe2/s2 (inorganic) cluster: L715 (= L214)
- binding uric acid: E773 (≠ V272), R851 (≠ A350), F885 (= F387), F980 (≠ K493), T981 (≠ N494), A1049 (= A573), A1050 (≠ G574), E1232 (= E760)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 44, 227, 228, 229, 230, 231, 232, 233, 234, 307, 312, 317, 320, 321, 323, 324, 330, 373, 374
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 111, 113, 145, 147
- binding nicotinamide-adenine-dinucleotide: 327, 363, 364, 428, 430, 431, 471, 478
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
23% identity, 93% coverage: 34:780/806 of query aligns to 561:1253/1295 of 6a7xA
- active site: Q740 (= Q237), E775 (≠ V272), R853 (≠ A350), H857 (= H354), R885 (= R384), G1233 (= G759), E1234 (= E760)
- binding bicarbonate ion: R812 (≠ A308), H813 (≠ R309), I850 (≠ K347), A883 (= A382), F884 (≠ Y383), F887 (= F387), G888 (≠ R388), Q891 (≠ E391)
- binding uric acid: E775 (≠ V272), R853 (≠ A350), F887 (= F387), F982 (≠ K493), T983 (≠ N494), A1052 (≠ G574), E1234 (= E760)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 314, 319, 322, 323, 325, 326, 332, 376
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 111, 113, 145, 147
- binding nicotinamide-adenine-dinucleotide: 329, 365, 366, 432, 433, 473, 480
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
23% identity, 93% coverage: 34:780/806 of query aligns to 559:1251/1286 of 4yswA
- active site: Q738 (= Q237), E773 (≠ V272), R851 (≠ A350), H855 (= H354), R883 (= R384), G1231 (= G759), E1232 (= E760)
- binding bicarbonate ion: R810 (≠ A308), H811 (≠ R309), I848 (≠ K347), T880 (≠ V381), A881 (= A382), F882 (≠ Y383), F885 (= F387), G886 (≠ R388), Q889 (≠ E391)
- binding calcium ion: G838 (≠ H336), T841 (≠ F339), E842 (≠ D340), S845 (≠ A343), S878 (≠ G379), N879 (≠ G380)
- binding fe2/s2 (inorganic) cluster: L715 (= L214)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S1196 (≠ M726)
- binding uric acid: E773 (≠ V272), R851 (≠ A350), F885 (= F387), F980 (≠ K493), T981 (≠ N494), A1050 (≠ G574), E1232 (= E760)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 44, 226, 227, 228, 229, 230, 231, 232, 233, 234, 307, 308, 312, 316, 317, 320, 321, 323, 324, 329, 330, 373, 374, 399
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 110, 111, 113, 145, 147
- binding 1,4-dihydronicotinamide adenine dinucleotide: 233, 326, 327, 328, 363, 364, 400, 401, 428, 430, 431, 471, 478
P22985 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Rattus norvegicus (Rat) (see 2 papers)
23% identity, 93% coverage: 34:780/806 of query aligns to 588:1280/1331 of P22985
- C992 (≠ T472) mutation to R: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with A-535. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and S-1316.
Sites not aligning to the query:
- 43 binding
- 48 binding
- 51 binding
- 73 binding
- 112 binding
- 115 binding
- 147 binding
- 149 binding
- 256:263 binding
- 335:336 WF→AL: Converts the enzyme to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents.
- 346:350 binding
- 359 binding
- 403 binding
- 535 C→A: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with R-992. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with R-992 and S-1316.
- 1316 C→S: Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and R-992.
Query Sequence
>3607804 FitnessBrowser__Dino:3607804
MNDMTPPTREERVEKLKGLGSSRKRVEDARFTQGKGNYVDDIKLPGMLHGDFVRSPYAHA
RVVSINAEAALALPGVVAVLTAKDLEPLSLHWMPTLAGDKQMVLADGKVLFQGQEVAFVV
AEDRYIAADAVELVEVEYEELPVLVDPFEALQSDVVLREDLEPGADGAHGPRRHHNHIFL
WEEGDKAATEQVIENAEVVVEEMVYYHRTHPCPLETCGSVASMDKVNGKLTLWGTFQAPH
VVRTVASLLSGIEEHNIRVISPDIGGGFGNKVGVYPGYVCSIVASIVTGKPVKFIEDRMD
NLMATAFARDYWMKGRISATKEGKITGLHCHVTADHGAFDACADPTKFPAGFFHICTGSY
DIPVAYVGVDGVYTNKAPGGVAYRCSFRVTEAAYFIERMIEVLAMELNMDAAELRRINFI
RKEQFPYTSALGWEYDSGDYHTAWDKALEAVDYKGLRAEQAERVEAFKRGETRKLLGIGL
THFTEIVGAGPVKNCDILGMGMFDSCEIRIHPTGSAVARLGTISQGQGHATTFAQILASE
TGIPADSITIEEGDTDTAPYGLGTYGSRSTPVAGAATALAGRKIRAKAQMIAAYLLEVHD
NDVEWDVDRFVVKGAPERFKTIQEIAYAAYNQAIPGVEPGLEAVSYYDPPNMTYPFGAYI
CVMEIDVDTGEHEIRQFYALDDCGTRINPMVIEGQVHGGLTEALAIAMGQEIAYDDIGNC
KTGTLMDFFIPTAWETPNYTTDFTETPSPHHPIGAKGVGESPNVGGVPAFSNAVHDAFRA
FGLRQSHMPHDHWRIWKTANQLGLHG
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