SitesBLAST
Comparing WP_011938850.1 NCBI__GCF_000016745.1:WP_011938850.1 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)
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
44% identity, 94% coverage: 23:425/427 of query aligns to 36:443/454 of O50131
- T92 (≠ I79) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (vs. gap) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G109) binding pyridoxal 5'-phosphate
- T125 (≠ A110) binding pyridoxal 5'-phosphate
- Q267 (= Q247) binding pyridoxal 5'-phosphate
- K293 (= K273) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T302) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
44% identity, 94% coverage: 23:425/427 of query aligns to 34:441/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ L50), S121 (= S108), G122 (= G109), T123 (≠ A110), F149 (= F136), H150 (= H137), R152 (= R139), E234 (= E216), D262 (= D244), V264 (= V246), Q265 (= Q247), K291 (= K273), N318 (≠ T301), T319 (= T302), R417 (= R401)
7vntA Structure of aminotransferase-substrate complex (see paper)
44% identity, 94% coverage: 23:425/427 of query aligns to 34:441/452 of 7vntA
- binding L-ornithine: F149 (= F136), R152 (= R139), E234 (= E216), K291 (= K273)
- binding pyridoxal-5'-phosphate: G122 (= G109), T123 (≠ A110), F149 (= F136), H150 (= H137), E229 (= E211), D262 (= D244), V264 (= V246), Q265 (= Q247), K291 (= K273)
7vnoA Structure of aminotransferase (see paper)
44% identity, 94% coverage: 23:425/427 of query aligns to 34:441/452 of 7vnoA
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
39% identity, 98% coverage: 7:425/427 of query aligns to 35:459/474 of O58478
- D251 (≠ E216) mutation to A: Loss of activity.
- K308 (= K273) mutation to A: Loss of activity.
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
40% identity, 93% coverage: 29:424/427 of query aligns to 28:419/421 of P50457
- K267 (= K273) mutation to A: No GABA-AT activity.
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
39% identity, 94% coverage: 22:423/427 of query aligns to 24:428/439 of 5wyaA
- active site: Y140 (≠ F136), E215 (= E211), D248 (= D244), N251 (≠ Q247), K278 (= K273), T307 (= T302), R406 (= R401)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ L50), Y82 (= Y80), S112 (= S108), G113 (= G109), S114 (≠ A110), Y140 (≠ F136), H141 (= H137), E215 (= E211), D248 (= D244), V250 (= V246), N251 (≠ Q247), K278 (= K273), F306 (≠ T301), T307 (= T302), R406 (= R401)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
39% identity, 94% coverage: 22:423/427 of query aligns to 26:430/446 of 5wyfA
- active site: Y142 (≠ F136), E217 (= E211), D250 (= D244), N253 (≠ Q247), K280 (= K273), T309 (= T302), R408 (= R401)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ L50), Y84 (= Y80), G115 (= G109), S116 (≠ A110), Y142 (≠ F136), H143 (= H137), D222 (≠ E216), D250 (= D244), V252 (= V246), N253 (≠ Q247), K280 (= K273), F308 (≠ T301), T309 (= T302), R408 (= R401)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
39% identity, 94% coverage: 22:423/427 of query aligns to 33:437/448 of 4ysnC
- active site: Y149 (≠ F136), E224 (= E211), D257 (= D244), N260 (≠ Q247), K287 (= K273), T316 (= T302), R415 (= R401)
- binding pyridoxal-5'-phosphate: S121 (= S108), G122 (= G109), S123 (≠ A110), Y149 (≠ F136), H150 (= H137), E224 (= E211), D257 (= D244), V259 (= V246), K287 (= K273), F315 (≠ T301), T316 (= T302)
Sites not aligning to the query:
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 99% coverage: 1:422/427 of query aligns to 1:419/426 of P22256
- I50 (≠ L50) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 109:110) binding pyridoxal 5'-phosphate
- E211 (= E216) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V246) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q247) binding pyridoxal 5'-phosphate
- K268 (= K273) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T302) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
39% identity, 97% coverage: 7:422/427 of query aligns to 6:418/425 of 1sffA
- active site: V18 (≠ L19), Y137 (≠ F136), E205 (= E211), D238 (= D244), Q241 (= Q247), K267 (= K273), T296 (= T302), R397 (= R401)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ G78), G110 (= G109), S111 (≠ A110), Y137 (≠ F136), H138 (= H137), R140 (= R139), E205 (= E211), D238 (= D244), V240 (= V246), Q241 (= Q247), K267 (= K273), T296 (= T302)
- binding sulfate ion: N152 (≠ V151), Y393 (≠ R397)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
39% identity, 97% coverage: 7:422/427 of query aligns to 6:418/425 of 1sf2A
- active site: V18 (≠ L19), Y137 (≠ F136), E205 (= E211), D238 (= D244), Q241 (= Q247), K267 (= K273), T296 (= T302), R397 (= R401)
- binding pyridoxal-5'-phosphate: G110 (= G109), S111 (≠ A110), Y137 (≠ F136), H138 (= H137), E205 (= E211), D238 (= D244), V240 (= V246), Q241 (= Q247), K267 (= K273)
- binding sulfate ion: N152 (≠ V151), Y393 (≠ R397)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
38% identity, 97% coverage: 7:422/427 of query aligns to 6:418/425 of 1szkA
- active site: V18 (≠ L19), Y137 (≠ F136), E205 (= E211), D238 (= D244), Q241 (= Q247), K267 (= K273), T296 (= T302), R397 (= R401)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G109), S111 (≠ A110), Y137 (≠ F136), H138 (= H137), E205 (= E211), D238 (= D244), V240 (= V246), Q241 (= Q247), K267 (= K273)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
40% identity, 98% coverage: 7:425/427 of query aligns to 23:442/444 of 4atqF
- active site: V35 (≠ L19), Y154 (≠ F136), E226 (= E211), D259 (= D244), Q262 (= Q247), K288 (= K273), T317 (= T302), R418 (= R401)
- binding gamma-amino-butanoic acid: M95 (≠ I79), Y154 (≠ F136), R157 (= R139), E231 (= E216), K288 (= K273), G316 (≠ T301)
- binding pyridoxal-5'-phosphate: G127 (= G109), A128 (= A110), Y154 (≠ F136), H155 (= H137), D259 (= D244), V261 (= V246)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
40% identity, 93% coverage: 24:420/427 of query aligns to 37:431/439 of 3q8nC
Sites not aligning to the query:
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
35% identity, 95% coverage: 23:427/427 of query aligns to 18:393/393 of 2ordA
- active site: F134 (= F136), E186 (= E211), D219 (= D244), Q222 (= Q247), K248 (= K273), T276 (= T302), R367 (= R401)
- binding pyridoxal-5'-phosphate: G102 (= G109), T103 (≠ A110), F134 (= F136), H135 (= H137), E186 (= E211), D219 (= D244), V221 (= V246), Q222 (= Q247), K248 (= K273)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
35% identity, 95% coverage: 23:427/427 of query aligns to 10:385/385 of Q9X2A5
- GT 94:95 (≠ GA 109:110) binding pyridoxal 5'-phosphate
- T268 (= T302) binding pyridoxal 5'-phosphate
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
37% identity, 94% coverage: 23:425/427 of query aligns to 24:410/412 of 2eo5A
- active site: F139 (= F136), E219 (= E211), D252 (= D244), Q255 (= Q247), K281 (= K273), T303 (= T302), R386 (= R401)
- binding pyridoxal-5'-phosphate: G113 (= G109), T114 (≠ A110), F139 (= F136), H140 (= H137), E219 (= E211), D252 (= D244), V254 (= V246), Q255 (= Q247), K281 (= K273)
Sites not aligning to the query:
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
37% identity, 96% coverage: 12:420/427 of query aligns to 32:431/440 of 6j2vA
- active site: L35 (≠ F15), Y154 (≠ F136), D256 (= D244), K285 (= K273)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G109), A128 (= A110), Y154 (≠ F136), H155 (= H137), R157 (= R139), E223 (= E211), E228 (= E216), D256 (= D244), I258 (≠ V246), K285 (= K273), G313 (≠ T301), T314 (= T302)
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
38% identity, 92% coverage: 24:417/427 of query aligns to 18:382/390 of 8ht4B
Query Sequence
>WP_011938850.1 NCBI__GCF_000016745.1:WP_011938850.1
METMAGLVNRAANVFTPALHLYYPVAIASGCGATVESTDGRLYLDFSSGLAVLNVGHNHP
RVLEAARKQLDCYIHTGGIYYSETSVSAAEKLVSITPDGLDMLFFSNSGAEAVEGALKLA
RFTTGRQGIISFTGAFHGRTLGAISLTTSSVDYRRRYHPLLPSVYHSPYPYCFRCPIHEC
PETCGLSCLRYLRTIFERQIPAEEVAAVIIEPVLGEGGYHPAPAKFLVELRKLCTEHGIL
LIFDEVQSGMGRTGRWFAGEQSGVVPDIMTVAKGIASGFPLSAVVAGRDLMQRWNPGAHG
TTFGGNPVSCAASIATIEVIQRQKLLDKASMGGVRALDRLRKIAATFPVIGDVRGFGHMI
GIEFVDKMGEPNGNACRKVLDHCLEKGLILIGCGPMRNIVRFIPPLVVSDAEMESALDIF
EQGVKGL
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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