SitesBLAST
Comparing WP_058931602.1 NCBI__GCF_001484605.1:WP_058931602.1 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)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
87% identity, 98% coverage: 8:455/456 of query aligns to 1:444/444 of 4atqF
- active site: V35 (= V42), Y154 (= Y161), E226 (= E233), D259 (= D266), Q262 (= Q269), K288 (= K295), T317 (= T324), R418 (= R429)
- binding gamma-amino-butanoic acid: M95 (= M102), Y154 (= Y161), R157 (= R164), E231 (= E238), K288 (= K295), G316 (= G323)
- binding pyridoxal-5'-phosphate: G127 (= G134), A128 (= A135), Y154 (= Y161), H155 (= H162), D259 (= D266), V261 (= V268)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
63% identity, 98% coverage: 8:453/456 of query aligns to 1:436/440 of 6j2vA
- active site: L35 (≠ V42), Y154 (= Y161), D256 (= D266), K285 (= K295)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G134), A128 (= A135), Y154 (= Y161), H155 (= H162), R157 (= R164), E223 (= E233), E228 (= E238), D256 (= D266), I258 (≠ V268), K285 (= K295), G313 (= G323), T314 (= T324)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
63% identity, 96% coverage: 12:450/456 of query aligns to 2:433/439 of 3q8nC
- active site: V32 (= V42), Y151 (= Y161), E221 (= E233), D254 (= D266), Q257 (= Q269), K283 (= K295), T312 (= T324), R412 (= R429)
- binding 4-oxobutanoic acid: G124 (= G134), A125 (= A135), V256 (= V268), K283 (= K295)
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, 92% coverage: 32:452/456 of query aligns to 8:419/421 of P50457
- K267 (= K295) mutation to A: No GABA-AT activity.
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
42% identity, 92% coverage: 30:449/456 of query aligns to 6:417/425 of 1sffA
- active site: V18 (= V42), Y137 (= Y161), E205 (= E233), D238 (= D266), Q241 (= Q269), K267 (= K295), T296 (= T324), R397 (= R429)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ M102), G110 (= G134), S111 (≠ A135), Y137 (= Y161), H138 (= H162), R140 (= R164), E205 (= E233), D238 (= D266), V240 (= V268), Q241 (= Q269), K267 (= K295), T296 (= T324)
- binding sulfate ion: N152 (≠ M176), Y393 (≠ G425)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
42% identity, 92% coverage: 30:449/456 of query aligns to 6:417/425 of 1sf2A
- active site: V18 (= V42), Y137 (= Y161), E205 (= E233), D238 (= D266), Q241 (= Q269), K267 (= K295), T296 (= T324), R397 (= R429)
- binding pyridoxal-5'-phosphate: G110 (= G134), S111 (≠ A135), Y137 (= Y161), H138 (= H162), E205 (= E233), D238 (= D266), V240 (= V268), Q241 (= Q269), K267 (= K295)
- binding sulfate ion: N152 (≠ M176), Y393 (≠ G425)
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)
42% identity, 92% coverage: 30:449/456 of query aligns to 7:418/426 of P22256
- I50 (= I73) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 134:135) binding pyridoxal 5'-phosphate
- E211 (= E238) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V268) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q269) binding pyridoxal 5'-phosphate
- K268 (= K295) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T324) binding pyridoxal 5'-phosphate
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
42% identity, 92% coverage: 30:449/456 of query aligns to 6:417/425 of 1szkA
- active site: V18 (= V42), Y137 (= Y161), E205 (= E233), D238 (= D266), Q241 (= Q269), K267 (= K295), T296 (= T324), R397 (= R429)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G134), S111 (≠ A135), Y137 (= Y161), H138 (= H162), E205 (= E233), D238 (= D266), V240 (= V268), Q241 (= Q269), K267 (= K295)
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)
36% identity, 95% coverage: 23:453/456 of query aligns to 28:459/474 of O58478
- D251 (≠ E238) mutation to A: Loss of activity.
- K308 (= K295) mutation to A: Loss of activity.
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)
37% identity, 97% coverage: 12:453/456 of query aligns to 1:443/454 of O50131
- T92 (≠ C100) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ F101) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G134) binding pyridoxal 5'-phosphate
- T125 (≠ A135) binding pyridoxal 5'-phosphate
- Q267 (= Q269) binding pyridoxal 5'-phosphate
- K293 (= K295) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T324) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
37% identity, 95% coverage: 21:453/456 of query aligns to 7:441/452 of 7vo1A