SitesBLAST
Comparing WP_011385299.1 NCBI__GCF_000009985.1:WP_011385299.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 hits to proteins with known functional sites (download)
8c0zB Cryoem structure of a tungsten-containing aldehyde oxidoreductase from aromatoleum aromaticum (see paper)
67% identity, 100% coverage: 1:616/616 of query aligns to 1:616/616 of 8c0zB
- binding magnesium ion: N92 (= N92), A182 (= A182)
- binding iron/sulfur cluster: R75 (= R75), C295 (= C294), C298 (= C297), C302 (= C301), C509 (= C509)
- binding tungsten cofactor: R75 (= R75), S91 (= S91), N92 (= N92), G94 (= G94), R181 (= R181), A182 (= A182), A183 (= A183), G184 (= G184), E329 (= E328), E331 (= E330), N356 (= N355), P362 (= P361), L465 (= L465), D504 (= D504), V510 (≠ I510), F511 (= F511)
8c0zA Cryoem structure of a tungsten-containing aldehyde oxidoreductase from aromatoleum aromaticum (see paper)
67% identity, 100% coverage: 1:616/616 of query aligns to 1:616/616 of 8c0zA
- binding iron/sulfur cluster: R181 (= R181), C295 (= C294), C298 (= C297), C302 (= C301), C509 (= C509)
- binding tungsten cofactor: R75 (= R75), N92 (= N92), G94 (= G94), R181 (= R181), A183 (= A183), G184 (= G184), R185 (= R185), E329 (= E328), E331 (= E330), N356 (= N355), P362 (= P361), L465 (= L465), D504 (= D504), V510 (≠ I510), F511 (= F511)
1aorA Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase (see paper)
49% identity, 100% coverage: 2:616/616 of query aligns to 4:602/605 of 1aorA
- binding fe (iii) ion: E332 (≠ F349), H383 (≠ V399)
- binding tungstopterin cofactor: R76 (= R75), A92 (≠ S91), N93 (= N92), G95 (= G94), R182 (= R181), A183 (= A182), G185 (= G184), R186 (= R185), E311 (= E328), E313 (= E330), D338 (≠ N355), D343 (= D360), T344 (≠ P361), R444 (= R460), H448 (= H464), I449 (≠ L465), K450 (≠ R466), D489 (= D504), C494 (= C509), L495 (≠ I510), F496 (= F511)
- binding iron/sulfur cluster: R76 (= R75), C288 (= C294), C291 (= C297), I293 (= I299), C295 (= C301), C494 (= C509), F496 (= F511)
1b4nA Formaldehyde ferredoxin oxidoreductase from pyrococcus furiosus, complexed with glutarate (see paper)
33% identity, 100% coverage: 3:615/616 of query aligns to 4:597/611 of 1b4nA
- binding calcium ion: G179 (≠ H180), E304 (≠ G326), D306 (≠ E328)
- binding glutaric acid: Y307 (= Y329), E308 (= E330), Y416 (= Y443), H437 (= H464), R473 (≠ T500), R484 (vs. gap)
- binding tungstopterin cofactor: K75 (≠ R75), G91 (≠ S91), N92 (= N92), L93 (≠ S93), G94 (= G94), R180 (= R181), A181 (= A182), A182 (= A183), G183 (= G184), R184 (= R185), D306 (≠ E328), E308 (= E330), N309 (≠ A331), D333 (≠ N355), M337 (≠ I359), D338 (= D360), T339 (≠ P361), H436 (≠ C463), H437 (= H464), K438 (≠ L465), F477 (= F503), E478 (≠ D504), A482 (≠ I508), C483 (= C509), R484 (vs. gap), L485 (vs. gap)
- binding iron/sulfur cluster: K75 (≠ R75), G283 (≠ A293), C284 (= C294), C287 (= C297), M289 (≠ I299), C291 (= C301), C483 (= C509), L485 (vs. gap)
1b25A Formaldehyde ferredoxin oxidoreductase from pyrococcus furiosus (see paper)
33% identity, 100% coverage: 3:615/616 of query aligns to 4:597/611 of 1b25A
- binding tungstopterin: K75 (≠ R75), G91 (≠ S91), N92 (= N92), L93 (≠ S93), G94 (= G94), G179 (≠ H180), R180 (= R181), A181 (= A182), G183 (= G184), R184 (= R185), T240 (= T242), E304 (≠ G326), D306 (≠ E328), Y307 (= Y329), E308 (= E330), N309 (≠ A331), D333 (≠ N355), D338 (= D360), T339 (≠ P361), I340 (= I362), H436 (≠ C463), H437 (= H464), K438 (≠ L465), E478 (≠ D504), A482 (≠ I508), C483 (= C509), R484 (vs. gap), L485 (vs. gap)
- binding iron/sulfur cluster: K75 (≠ R75), R180 (= R181), C284 (= C294), C287 (= C297), M289 (≠ I299), C291 (= C301), C483 (= C509)
6x1oC Wor5 from pyrococcus furiosus, as crystallized (see paper)
30% identity, 99% coverage: 2:613/616 of query aligns to 3:606/624 of 6x1oC
- binding magnesium ion: M194 (≠ H180), D323 (≠ S316), D326 (≠ E328)
- binding phosphate ion: R249 (≠ P238), Y296 (≠ N291)
- binding tungstopterin cofactor: K77 (≠ R75), S93 (= S91), V94 (≠ N92), L95 (≠ S93), S96 (≠ G94), H195 (≠ R181), A196 (= A182), A197 (= A183), G198 (= G184), Y199 (≠ R185), D326 (≠ E328), E328 (= E330), D353 (≠ N355), D358 (= D360), G359 (≠ P361), I360 (= I362), H469 (= H464), T470 (≠ S472), Y489 (≠ F503), D490 (= D504), I494 (= I508), C495 (= C509), N496 (≠ I510), F497 (= F511)
- binding iron/sulfur cluster: S96 (≠ G94), D299 (≠ C294), C302 (= C297), C306 (= C301), C495 (= C509), F497 (= F511), V498 (≠ T512)
- binding (1R)-1-hydroxybutane-1-sulfonic acid: T253 (= T242), Y327 (= Y329), E328 (= E330), H446 (≠ Y443), H469 (= H464)
4z3zA Active site complex bambc of benzoyl coenzyme a reductase in complex with zinc (see paper)
32% identity, 68% coverage: 4:419/616 of query aligns to 6:409/652 of 4z3zA
Sites not aligning to the query:
4z3yA Active site complex bambc of benzoyl coenzyme a reductase in complex with benzoyl-coa (see paper)
32% identity, 68% coverage: 4:419/616 of query aligns to 6:409/653 of 4z3yA
Sites not aligning to the query:
4z3wC Active site complex bambc of benzoyl coenzyme a reductase in complex with 1,5 dienoyl-coa (see paper)
32% identity, 68% coverage: 4:419/616 of query aligns to 6:409/653 of 4z3wC
- binding 1,5 Dienoyl-CoA: P249 (≠ Q243), W259 (≠ G253), H260 (≠ A254), F323 (vs. gap)
- binding magnesium ion: M94 (≠ N92), S183 (≠ A182)
- binding iron/sulfur cluster: R77 (= R75), R181 (≠ H180), C299 (= C294), C302 (= C297), M304 (≠ I299), C306 (= C301)
Sites not aligning to the query:
- binding 1,5 Dienoyl-CoA: 436, 438, 439, 440, 445, 458, 461, 466, 499, 500, 504
- binding iron/sulfur cluster: 534
Query Sequence
>WP_011385299.1 NCBI__GCF_000009985.1:WP_011385299.1
MSWTGKFLRIDLTNGSVKTEELNRAWARQYLGQRGLATKYFAEEVDPKVDPLSPANKMIF
TTGPLTGTAASTGGRYSVVTKGPLTNCIACSNSGGFFGNELKNAGWDMIIVEGRSPKPVY
LSIENETVEIRDAAEFWGKTVWETENGLKARHQDPMLRVATIGAAGEKGVLYACIVNDLH
RAAGRSGVGAVMGSKNLKAIAVRGTRGVTVKDPDRFIKATIEQKKVLADNAVTGQGLPKY
GTQVLMNVINEIGAMPTRNFKEVQFEGAHKISAEAMHEPRATDGKANLATNGACFGCTIA
CGRISRMDPGHFSITSRPQYKEPSGGVEYEAAWAMGSDCGVDDLEACTFANFMCNEHGID
PISFGSTLAAAMEMFEMGVITKEQTGGVELKFGSAEALVKMAELTGKGEGFGLELGQGSR
RLCAKYGHPELSMTVKSQEFPAYDPRGIQGMGLTYATSNRGACHLRSYTVASEVLGIPFK
SDPLATDGKAALVKAFQDATAAFDASGICIFTTFAWSLENLAPQIDAACEGEWTPEILLE
VGERIWTLERQFNLAAGMTAADDTLPKRLLKDAAKTGPAKGLTSGLEKMLPEYYQLRGWT
TDGVPTTETLKRLQLA
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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