SitesBLAST
Comparing WP_027723350.1 NCBI__GCF_000425265.1:WP_027723350.1 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)
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)
47% identity, 100% coverage: 1:430/432 of query aligns to 1:423/426 of P22256
- I50 (= I50) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 111:112) binding pyridoxal 5'-phosphate
- E211 (= E218) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I248) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q249) binding pyridoxal 5'-phosphate
- K268 (= K275) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T304) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
47% identity, 99% coverage: 2:430/432 of query aligns to 1:422/425 of 1sffA
- active site: V18 (= V19), Y137 (≠ F138), E205 (= E213), D238 (= D246), Q241 (= Q249), K267 (= K275), T296 (= T304), R397 (= R405)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ H79), G110 (= G111), S111 (≠ A112), Y137 (≠ F138), H138 (= H139), R140 (= R141), E205 (= E213), D238 (= D246), V240 (≠ I248), Q241 (= Q249), K267 (= K275), T296 (= T304)
- binding sulfate ion: N152 (≠ K153), Y393 (≠ G401)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
47% identity, 99% coverage: 2:430/432 of query aligns to 1:422/425 of 1sf2A
- active site: V18 (= V19), Y137 (≠ F138), E205 (= E213), D238 (= D246), Q241 (= Q249), K267 (= K275), T296 (= T304), R397 (= R405)
- binding pyridoxal-5'-phosphate: G110 (= G111), S111 (≠ A112), Y137 (≠ F138), H138 (= H139), E205 (= E213), D238 (= D246), V240 (≠ I248), Q241 (= Q249), K267 (= K275)
- binding sulfate ion: N152 (≠ K153), Y393 (≠ G401)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
47% identity, 99% coverage: 2:430/432 of query aligns to 1:422/425 of 1szkA
- active site: V18 (= V19), Y137 (≠ F138), E205 (= E213), D238 (= D246), Q241 (= Q249), K267 (= K275), T296 (= T304), R397 (= R405)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G111), S111 (≠ A112), Y137 (≠ F138), H138 (= H139), E205 (= E213), D238 (= D246), V240 (≠ I248), Q241 (= Q249), K267 (= K275)
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)
43% identity, 99% coverage: 1:428/432 of query aligns to 1:419/421 of P50457
- K267 (= K275) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
46% identity, 99% coverage: 4:430/432 of query aligns to 17:437/439 of 3q8nC
- active site: V32 (= V19), Y151 (≠ F138), E221 (= E213), D254 (= D246), Q257 (= Q249), K283 (= K275), T312 (= T304), R412 (= R405)
- binding 4-oxobutanoic acid: G124 (= G111), A125 (= A112), V256 (≠ I248), K283 (= K275)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
47% identity, 99% coverage: 3:428/432 of query aligns to 19:441/444 of 4atqF
- active site: V35 (= V19), Y154 (≠ F138), E226 (= E213), D259 (= D246), Q262 (= Q249), K288 (= K275), T317 (= T304), R418 (= R405)
- binding gamma-amino-butanoic acid: M95 (≠ H79), Y154 (≠ F138), R157 (= R141), E231 (= E218), K288 (= K275), G316 (= G303)
- binding pyridoxal-5'-phosphate: G127 (= G111), A128 (= A112), Y154 (≠ F138), H155 (= H139), D259 (= D246), V261 (≠ I248)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
44% identity, 100% coverage: 3:432/432 of query aligns to 19:439/440 of 6j2vA
- active site: L35 (≠ V19), Y154 (≠ F138), D256 (= D246), K285 (= K275)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G111), A128 (= A112), Y154 (≠ F138), H155 (= H139), R157 (= R141), E223 (= E213), E228 (= E218), D256 (= D246), I258 (= I248), K285 (= K275), G313 (= G303), T314 (= T304)
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)
39% identity, 99% coverage: 3:428/432 of query aligns to 14:442/454 of O50131
- T92 (≠ I80) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ A81) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G111) binding pyridoxal 5'-phosphate
- T125 (≠ A112) binding pyridoxal 5'-phosphate
- Q267 (= Q249) binding pyridoxal 5'-phosphate
- K293 (= K275) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T304) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
39% identity, 99% coverage: 3:428/432 of query aligns to 12:440/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I50), S121 (= S110), G122 (= G111), T123 (≠ A112), F149 (= F138), H150 (= H139), R152 (= R141), E234 (= E218), D262 (= D246), V264 (≠ I248), Q265 (= Q249), K291 (= K275), N318 (≠ G303), T319 (= T304), R417 (= R405)
7vntA Structure of aminotransferase-substrate complex (see paper)
39% identity, 99% coverage: 3:428/432 of query aligns to 12:440/452 of 7vntA
- binding L-ornithine: F149 (= F138), R152 (= R141), E234 (= E218), K291 (= K275)
- binding pyridoxal-5'-phosphate: G122 (= G111), T123 (≠ A112), F149 (= F138), H150 (= H139), E229 (= E213), D262 (= D246), V264 (≠ I248), Q265 (= Q249), K291 (= K275)
7vnoA Structure of aminotransferase (see paper)
39% identity, 99% coverage: 3:428/432 of query aligns to 12:440/452 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)
37% identity, 99% coverage: 3:428/432 of query aligns to 31:458/474 of O58478
- D251 (≠ E218) mutation to A: Loss of activity.
- K308 (= K275) mutation to A: Loss of activity.
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
34% identity, 99% coverage: 1:428/432 of query aligns to 2:429/439 of 5wyaA
- active site: A20 (≠ V19), Y140 (≠ F138), E215 (= E213), D248 (= D246), N251 (≠ Q249), K278 (= K275), T307 (= T304), R406 (= R405)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I50), Y82 (≠ I80), S112 (= S110), G113 (= G111), S114 (≠ A112), Y140 (≠ F138), H141 (= H139), E215 (= E213), D248 (= D246), V250 (≠ I248), N251 (≠ Q249), K278 (= K275), F306 (≠ G303), T307 (= T304), R406 (= R405)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
34% identity, 99% coverage: 1:428/432 of query aligns to 11:438/448 of 4ysnC
- active site: A29 (≠ V19), Y149 (≠ F138), E224 (= E213), D257 (= D246), N260 (≠ Q249), K287 (= K275), T316 (= T304), R415 (= R405)
- binding pyridoxal-5'-phosphate: S121 (= S110), G122 (= G111), S123 (≠ A112), Y149 (≠ F138), H150 (= H139), E224 (= E213), D257 (= D246), V259 (≠ I248), K287 (= K275), F315 (≠ G303), T316 (= T304)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
34% identity, 99% coverage: 1:428/432 of query aligns to 4:431/446 of 5wyfA
- active site: A22 (≠ V19), Y142 (≠ F138), E217 (= E213), D250 (= D246), N253 (≠ Q249), K280 (= K275), T309 (= T304), R408 (= R405)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I50), Y84 (≠ I80), G115 (= G111), S116 (≠ A112), Y142 (≠ F138), H143 (= H139), D222 (≠ E218), D250 (= D246), V252 (≠ I248), N253 (≠ Q249), K280 (= K275), F308 (≠ G303), T309 (= T304), R408 (= R405)
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
35% identity, 94% coverage: 22:428/432 of query aligns to 23:409/412 of 2eo5A
- active site: F139 (= F138), E219 (= E213), D252 (= D246), Q255 (= Q249), K281 (= K275), T303 (= T304), R386 (= R405)
- binding pyridoxal-5'-phosphate: G113 (= G111), T114 (≠ A112), F139 (= F138), H140 (= H139), E219 (= E213), D252 (= D246), V254 (≠ I248), Q255 (= Q249), K281 (= K275)
Sites not aligning to the query:
1zobA Crystal structure of dialkylglycine decarboxylases bound with calcium ion
33% identity, 97% coverage: 11:428/432 of query aligns to 12:427/431 of 1zobA
- active site: G19 (= G18), W136 (≠ F138), E208 (= E213), D241 (= D246), Q244 (= Q249), K270 (= K275), T301 (= T304), R404 (= R405)
- binding calcium ion: L76 (≠ C77), S78 (≠ H79), V303 (≠ G306), S304 (≠ G307), D305 (≠ N308)
- binding pyridoxal-5'-phosphate: T108 (≠ S110), A110 (= A112), N113 (≠ V115), W136 (≠ F138), H137 (= H139), E208 (= E213), D241 (= D246), A243 (≠ I248), Q244 (= Q249), K270 (= K275)
1zc9A The crystal structure of dialkylglycine decarboxylase complex with pyridoxamine 5-phosphate (see paper)
33% identity, 97% coverage: 11:428/432 of query aligns to 12:427/431 of 1zc9A
- active site: G19 (= G18), W136 (≠ F138), E208 (= E213), D241 (= D246), Q244 (= Q249), K270 (= K275), T301 (= T304), R404 (= R405)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G109 (= G111), A110 (= A112), W136 (≠ F138), H137 (= H139), E208 (= E213), D241 (= D246), A243 (≠ I248), Q244 (= Q249), K270 (= K275)
1m0qA Structure of dialkylglycine decarboxylase complexed with s-1- aminoethanephosphonate (see paper)
33% identity, 97% coverage: 11:428/432 of query aligns to 12:427/431 of 1m0qA
- active site: G19 (= G18), W136 (≠ F138), E208 (= E213), D241 (= D246), Q244 (= Q249), K270 (= K275), T301 (= T304), R404 (= R405)
- binding (1s)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]ethylphosphonic acid: Q50 (≠ I50), T108 (≠ S110), A110 (= A112), W136 (≠ F138), H137 (= H139), E208 (= E213), S213 (≠ E218), D241 (= D246), A243 (≠ I248), Q244 (= Q249), K270 (= K275), R404 (= R405)
Query Sequence
>WP_027723350.1 NCBI__GCF_000425265.1:WP_027723350.1
MSKSETLLERRNKAVALGVGNLAPVFADRAQNSVVTDVDGNEYIDFVGGIGVNNVGHCNE
KVVAAIKEQAEKLIHSCFHIAMYESYIALAEKLIEITPGDFEKKAVLLNSGAEAVENAVK
ISRLASGKSGIIVYEGGFHGRTLLTMSMTSKVKPYKFKFGPYAPEIYRIPYPYCYRCPYG
KEYPSCDIHCAEQLKSWFIGNAAPENIAAIVAEPIAGEGGFLTPPPEYFPRIKEICADNG
IYFVADEIQTGGGRTGKFCAIDHWGVEPDLMTMAKSIGGGMPISAVVGRKEIMDAVHPGG
LGGTYGGNPVSCAAALAAINALENEGILEKGQALGKKVKDVFNSWKKKYSIIGDVRGLGA
MIALEIVTDKDSKTPAPDLTKKIVAEAVKNKLLILSCGNFGNVIRILVPLSVDDQTLDKG
LSILEKAIIEQS
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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