SitesBLAST
Comparing 206619 MicrobesOnline__882:206619 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)
36% identity, 97% coverage: 3:558/576 of query aligns to 7:561/605 of 1aorA
- binding fe (iii) ion: E332 (≠ R340), H383 (≠ L377)
- binding tungstopterin cofactor: R76 (= R69), A92 (≠ S85), N93 (= N86), G95 (= G88), R182 (= R182), A183 (= A183), G185 (= G185), R186 (= R186), E311 (= E319), E313 (= E321), D338 (= D346), D343 (= D351), T344 (= T352), R444 (≠ M438), H448 (= H442), I449 (≠ T443), K450 (≠ A444), D489 (= D482), C494 (= C487), L495 (= L488), F496 (= F489)
- binding iron/sulfur cluster: R76 (= R69), C288 (= C294), C291 (= C298), I293 (= I300), C295 (= C302), C494 (= C487), F496 (= F489)
8c0zB Cryoem structure of a tungsten-containing aldehyde oxidoreductase from aromatoleum aromaticum (see paper)
32% identity, 96% coverage: 3:556/576 of query aligns to 6:573/616 of 8c0zB
- binding magnesium ion: N92 (= N86), A182 (= A183)
- binding iron/sulfur cluster: R75 (= R69), C295 (≠ H295), C298 (= C298), C302 (= C302), C509 (= C487)
- binding tungsten cofactor: R75 (= R69), S91 (= S85), N92 (= N86), G94 (= G88), R181 (= R182), A182 (= A183), A183 (= A184), G184 (= G185), E329 (= E319), E331 (= E321), N356 (≠ D346), P362 (≠ T352), L465 (≠ T443), D504 (= D482), V510 (≠ L488), F511 (= F489)
8c0zA Cryoem structure of a tungsten-containing aldehyde oxidoreductase from aromatoleum aromaticum (see paper)
32% identity, 96% coverage: 3:556/576 of query aligns to 6:573/616 of 8c0zA
- binding iron/sulfur cluster: R181 (= R182), C295 (≠ H295), C298 (= C298), C302 (= C302), C509 (= C487)
- binding tungsten cofactor: R75 (= R69), N92 (= N86), G94 (= G88), R181 (= R182), A183 (= A184), G184 (= G185), R185 (= R186), E329 (= E319), E331 (= E321), N356 (≠ D346), P362 (≠ T352), L465 (≠ T443), D504 (= D482), V510 (≠ L488), F511 (= F489)
1b4nA Formaldehyde ferredoxin oxidoreductase from pyrococcus furiosus, complexed with glutarate (see paper)
32% identity, 78% coverage: 3:452/576 of query aligns to 7:447/611 of 1b4nA
- binding calcium ion: G179 (≠ A181), E304 (≠ G317), D306 (≠ E319)
- binding glutaric acid: Y307 (= Y320), E308 (= E321), Y416 (= Y421), H437 (= H442)
- binding tungstopterin cofactor: K75 (≠ R69), G91 (≠ S85), N92 (= N86), L93 (≠ S87), G94 (= G88), R180 (= R182), A181 (= A183), A182 (= A184), G183 (= G185), R184 (= R186), D306 (≠ E319), E308 (= E321), N309 (≠ T322), D333 (= D346), M337 (≠ V350), D338 (= D351), T339 (= T352), H436 (≠ D441), H437 (= H442), K438 (≠ T443)
- binding iron/sulfur cluster: K75 (≠ R69), G283 (≠ C294), C284 (≠ H295), C287 (= C298), M289 (≠ I300), C291 (= C302)
Sites not aligning to the query:
1b25A Formaldehyde ferredoxin oxidoreductase from pyrococcus furiosus (see paper)
32% identity, 78% coverage: 3:452/576 of query aligns to 7:447/611 of 1b25A
- binding tungstopterin: K75 (≠ R69), G91 (≠ S85), N92 (= N86), L93 (≠ S87), G94 (= G88), G179 (≠ A181), R180 (= R182), A181 (= A183), G183 (= G185), R184 (= R186), T240 (= T245), E304 (≠ G317), D306 (≠ E319), Y307 (= Y320), E308 (= E321), N309 (≠ T322), D333 (= D346), D338 (= D351), T339 (= T352), I340 (= I353), H436 (≠ D441), H437 (= H442), K438 (≠ T443)
- binding iron/sulfur cluster: K75 (≠ R69), R180 (= R182), C284 (≠ H295), C287 (= C298), M289 (≠ I300), C291 (= C302)
Sites not aligning to the query:
6x1oC Wor5 from pyrococcus furiosus, as crystallized (see paper)
24% identity, 93% coverage: 26:558/576 of query aligns to 33:565/624 of 6x1oC
- binding magnesium ion: M194 (≠ A181), D323 (≠ S316), D326 (≠ E319)
- binding phosphate ion: R249 (≠ T236), Y296 (≠ E292)
- binding tungstopterin cofactor: K77 (≠ R69), S93 (= S85), V94 (≠ N86), L95 (≠ S87), S96 (≠ G88), H195 (≠ R182), A196 (= A183), A197 (= A184), G198 (= G185), Y199 (≠ R186), D326 (≠ E319), E328 (= E321), D353 (= D346), D358 (= D351), G359 (≠ T352), I360 (= I353), H469 (= H442), T470 (= T443), Y489 (≠ V481), D490 (= D482), I494 (≠ L486), C495 (= C487), N496 (≠ L488), F497 (= F489)
- binding iron/sulfur cluster: S96 (≠ G88), D299 (≠ H295), C302 (= C298), C306 (= C302), C495 (= C487), F497 (= F489), V498 (= V490)
- binding (1R)-1-hydroxybutane-1-sulfonic acid: T253 (≠ Q238), Y327 (= Y320), E328 (= E321), H446 (≠ Y421), H469 (= H442)
4z3zA Active site complex bambc of benzoyl coenzyme a reductase in complex with zinc (see paper)
26% identity, 66% coverage: 25:406/576 of query aligns to 33:417/652 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)
26% identity, 66% coverage: 25:406/576 of query aligns to 33:417/653 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)
26% identity, 66% coverage: 25:406/576 of query aligns to 33:417/653 of 4z3wC
- binding 1,5 Dienoyl-CoA: P249 (≠ A246), W259 (≠ F258), H260 (≠ P259), F323 (= F318)
- binding magnesium ion: M94 (≠ N86), S183 (≠ A183)
- binding iron/sulfur cluster: R77 (= R69), R181 (= R179), C299 (= C294), C302 (= C298), M304 (≠ I300), C306 (= C302)
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
>206619 MicrobesOnline__882:206619
MPRILRINTRERSWRFEEPGKYAGLGGRSLTSRLVQDEVPADTHALSAENRIVAAIGLLS
GTGAANSGRISIGAKSPLTGGIKESNSGGSFCQKLARLDILALVLEDKPEPNAPLVNIVL
TKDGVRFDEAGDMAGKGTYACMDAVSERYGKKACAMLIGPAGESLLTGASIQFSDPWGRP
ARAAGRGGLGAVMGSKRVKAIVIDDEGGTRFGYADEARFKAASKRWAEILRAHPVTGQGL
PGFGTAILVNIINEAGAFPTQNFRTGRCEHAPKISGEVMAEYMEKRGGKVKEGCHAGCII
QCSQNYVDPAGEYITSGFEYETVWAFGGNSLIADIDDIARLDRMCDDLGVDTIEIGNTVA
IAMDAGIIPWGDGKAALKLLARIADPSDALGRIIGSGVGFAAQAFGIDRVPTVKNQSMPA
YDPRAAKGVGVTYATTTMGADHTAGYAICQNMLKVGGDVNPLGKEGQVETSKALQVATAT
VDSLGLCLFVAFAVLDTPDAVQCICDMVSARHGIDFTPNDFIAIGTDVLKVEQKFNADAG
FTPEDDQLPAFMKREPLPPHNVVWDFSVEELQQAKV
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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