SitesBLAST
Comparing WP_011383898.1 NCBI__GCF_000009985.1:WP_011383898.1 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)
1aorA Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase (see paper)
33% identity, 95% coverage: 5:547/569 of query aligns to 9:561/605 of 1aorA
- binding fe (iii) ion: E332 (≠ R340), H383 (≠ A377)
- binding tungstopterin cofactor: R76 (= R70), A92 (= A86), N93 (= N87), G95 (= G89), R182 (= R181), A183 (≠ L182), G185 (≠ A184), R186 (= R185), E311 (= E319), E313 (= E321), D338 (≠ N346), D343 (= D351), T344 (= T352), R444 (≠ Q437), H448 (= H441), I449 (≠ T442), K450 (≠ T443), D489 (= D474), C494 (= C479), L495 (≠ V480), F496 (= F481)
- binding iron/sulfur cluster: R76 (= R70), C288 (≠ S291), C291 (= C294), I293 (≠ P296), C295 (= C298), C494 (= C479), F496 (= F481)
1b4nA Formaldehyde ferredoxin oxidoreductase from pyrococcus furiosus, complexed with glutarate (see paper)
31% identity, 77% coverage: 5:441/569 of query aligns to 9:437/611 of 1b4nA
- binding calcium ion: G179 (≠ A180), E304 (≠ P317), D306 (≠ E319)
- binding glutaric acid: Y307 (= Y320), E308 (= E321), Y416 (= Y420), H437 (= H441)
- binding tungstopterin cofactor: K75 (≠ R70), G91 (≠ A86), N92 (= N87), L93 (≠ T88), G94 (= G89), R180 (= R181), A181 (≠ L182), A182 (= A183), G183 (≠ A184), R184 (= R185), D306 (≠ E319), E308 (= E321), N309 (≠ T322), D333 (≠ N346), M337 (≠ I350), D338 (= D351), T339 (= T352), H436 (≠ D440), H437 (= H441)
- binding iron/sulfur cluster: K75 (≠ R70), G283 (≠ A293), C284 (= C294), C287 (= C298), M289 (≠ I300), C291 (= C302)
Sites not aligning to the query:
1b25A Formaldehyde ferredoxin oxidoreductase from pyrococcus furiosus (see paper)
31% identity, 77% coverage: 5:441/569 of query aligns to 9:437/611 of 1b25A
- binding tungstopterin: K75 (≠ R70), G91 (≠ A86), N92 (= N87), L93 (≠ T88), G94 (= G89), G179 (≠ A180), R180 (= R181), A181 (≠ L182), G183 (≠ A184), R184 (= R185), T240 (= T241), E304 (≠ P317), D306 (≠ E319), Y307 (= Y320), E308 (= E321), N309 (≠ T322), D333 (≠ N346), D338 (= D351), T339 (= T352), I340 (= I353), H436 (≠ D440), H437 (= H441)
- binding iron/sulfur cluster: K75 (≠ R70), R180 (= R181), C284 (= C294), C287 (= C298), M289 (≠ I300), C291 (= C302)
Sites not aligning to the query:
8c0zB Cryoem structure of a tungsten-containing aldehyde oxidoreductase from aromatoleum aromaticum (see paper)
28% identity, 94% coverage: 2:538/569 of query aligns to 5:566/616 of 8c0zB
- binding magnesium ion: N92 (= N87), A182 (≠ L182)
- binding iron/sulfur cluster: R75 (= R70), C295 (≠ M295), C298 (= C298), C302 (= C302), C509 (= C479)
- binding tungsten cofactor: R75 (= R70), S91 (≠ A86), N92 (= N87), G94 (= G89), R181 (= R181), A182 (≠ L182), A183 (= A183), G184 (≠ A184), E329 (= E319), E331 (= E321), N356 (= N346), P362 (≠ T352), L465 (≠ T442), D504 (= D474), V510 (= V480), F511 (vs. gap)
8c0zA Cryoem structure of a tungsten-containing aldehyde oxidoreductase from aromatoleum aromaticum (see paper)
28% identity, 94% coverage: 2:538/569 of query aligns to 5:566/616 of 8c0zA
- binding iron/sulfur cluster: R181 (= R181), C295 (≠ M295), C298 (= C298), C302 (= C302), C509 (= C479)
- binding tungsten cofactor: R75 (= R70), N92 (= N87), G94 (= G89), R181 (= R181), A183 (= A183), G184 (≠ A184), R185 (= R185), E329 (= E319), E331 (= E321), N356 (= N346), P362 (≠ T352), L465 (≠ T442), D504 (= D474), V510 (= V480), F511 (vs. gap)
6x1oC Wor5 from pyrococcus furiosus, as crystallized (see paper)
25% identity, 95% coverage: 5:547/569 of query aligns to 9:565/624 of 6x1oC
- binding magnesium ion: M194 (≠ A180), D323 (≠ V315), D326 (≠ E319)
- binding phosphate ion: R249 (≠ K237), Y296 (≠ G288)
- binding tungstopterin cofactor: K77 (≠ R70), S93 (≠ A86), V94 (≠ N87), L95 (≠ T88), S96 (≠ G89), H195 (≠ R181), A196 (≠ L182), A197 (= A183), G198 (≠ A184), Y199 (≠ R185), D326 (≠ E319), E328 (= E321), D353 (≠ N346), D358 (= D351), G359 (≠ T352), I360 (= I353), H469 (= H441), T470 (= T442), Y489 (≠ A473), D490 (= D474), I494 (≠ L478), C495 (= C479), N496 (≠ V480), F497 (= F481)
- binding iron/sulfur cluster: S96 (≠ G89), D299 (≠ S291), C302 (= C294), C306 (= C298), C495 (= C479), F497 (= F481), V498 (= V485)
- binding (1R)-1-hydroxybutane-1-sulfonic acid: T253 (= T241), Y327 (= Y320), E328 (= E321), H446 (≠ Y420), H469 (= H441)
4z3zA Active site complex bambc of benzoyl coenzyme a reductase in complex with zinc (see paper)
32% identity, 36% coverage: 5:206/569 of query aligns to 10:207/652 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, 36% coverage: 5:206/569 of query aligns to 10:207/653 of 4z3yA
Sites not aligning to the query:
- binding benzoyl coenzyme A: 249, 259, 323, 436, 439, 440, 445, 458, 461, 466, 500, 504
- binding iron/sulfur cluster: 299, 302, 304, 305, 306, 534
4z3wC Active site complex bambc of benzoyl coenzyme a reductase in complex with 1,5 dienoyl-coa (see paper)
32% identity, 36% coverage: 5:206/569 of query aligns to 10:207/653 of 4z3wC
Sites not aligning to the query:
- binding 1,5 Dienoyl-CoA: 249, 259, 260, 323, 436, 438, 439, 440, 445, 458, 461, 466, 499, 500, 504
- binding iron/sulfur cluster: 299, 302, 304, 306, 534
Query Sequence
>WP_011383898.1 NCBI__GCF_000009985.1:WP_011383898.1
MRTHLHVDLTSRTITKAEIRGDDLARAGRYLIARTLLESGVARVDPLGPDNPLIFSAGPY
AGTNLSNANRLSVGCKSPLTGGIKEANTGGTFAVALGQLALAGLTLHGCCDEWVVIRITK
EGDITFTSAEPYLGKGTFEVAAMLHEAYGKKVSIAQCGPVGERLGLLGGISFSDREGRPA
RLAARGGVGAVMGSKKVKAIVVDLTKIPELHDRAKVMASTKDYAAKLSEQAPVKAMKERG
TAMVGDFTNYVGGMPVRNFSAGQLVDPKVEPLKVGGDYIRERNMGRGGNPSHACMPGCVI
QCSNEYVDENGKELVSPLEYETLGLLGTNCGLDDPDDIARLNYICNDLGIDTIETGATMG
VLMEAGQGAFGDVGFVAQALADIGAGNERGRLLAQGTARVGEHYGVRRVPVIKKQAISAY
DPRVIEVTGVSMMTTAQGADHTTGNLPMMDTKDKSVAEVVEASITAQINAAIADSLGLCV
FGRSVTDTNRQLLAEAVNACHGTSIDPEFFLEIGRETLRLEHRFNQEAGFLTADDELPRF
FLDEALPPTNKVARFHAEEVGRHMAGLFG
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