SitesBLAST
Comparing WP_068170823.1 NCBI__GCF_001592305.1:WP_068170823.1 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)
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)
61% identity, 97% coverage: 9:425/428 of query aligns to 2:421/421 of P50457
- K267 (= K272) mutation to A: No GABA-AT activity.
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)
51% identity, 98% coverage: 8:425/428 of query aligns to 2:423/426 of P22256
- I50 (= I56) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 117:118) binding pyridoxal 5'-phosphate
- E211 (= E215) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V245) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q246) binding pyridoxal 5'-phosphate
- K268 (= K272) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T301) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
51% identity, 98% coverage: 8:425/428 of query aligns to 1:422/425 of 1sffA
- active site: V18 (= V25), Y137 (≠ F144), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T301), R397 (= R400)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q85), G110 (= G117), S111 (≠ A118), Y137 (≠ F144), H138 (= H145), R140 (= R147), E205 (= E210), D238 (= D243), V240 (= V245), Q241 (= Q246), K267 (= K272), T296 (= T301)
- binding sulfate ion: N152 (≠ Q159), Y393 (≠ G396)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
51% identity, 98% coverage: 8:425/428 of query aligns to 1:422/425 of 1sf2A
- active site: V18 (= V25), Y137 (≠ F144), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T301), R397 (= R400)
- binding pyridoxal-5'-phosphate: G110 (= G117), S111 (≠ A118), Y137 (≠ F144), H138 (= H145), E205 (= E210), D238 (= D243), V240 (= V245), Q241 (= Q246), K267 (= K272)
- binding sulfate ion: N152 (≠ Q159), Y393 (≠ G396)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
51% identity, 98% coverage: 8:425/428 of query aligns to 1:422/425 of 1szkA
- active site: V18 (= V25), Y137 (≠ F144), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T301), R397 (= R400)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G117), S111 (≠ A118), Y137 (≠ F144), H138 (= H145), E205 (= E210), D238 (= D243), V240 (= V245), Q241 (= Q246), K267 (= K272)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
48% identity, 96% coverage: 16:425/428 of query aligns to 23:437/439 of 3q8nC
- active site: V32 (= V25), Y151 (≠ F144), E221 (= E210), D254 (= D243), Q257 (= Q246), K283 (= K272), T312 (= T301), R412 (= R400)
- binding 4-oxobutanoic acid: G124 (= G117), A125 (= A118), V256 (= V245), K283 (= K272)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
43% identity, 96% coverage: 12:423/428 of query aligns to 22:435/440 of 6j2vA
- active site: L35 (≠ V25), Y154 (≠ F144), D256 (= D243), K285 (= K272)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G117), A128 (= A118), Y154 (≠ F144), H155 (= H145), R157 (= R147), E223 (= E210), E228 (= E215), D256 (= D243), I258 (≠ V245), K285 (= K272), G313 (= G300), T314 (= T301)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
43% identity, 96% coverage: 12:423/428 of query aligns to 22:441/444 of 4atqF
- active site: V35 (= V25), Y154 (≠ F144), E226 (= E210), D259 (= D243), Q262 (= Q246), K288 (= K272), T317 (= T301), R418 (= R400)
- binding gamma-amino-butanoic acid: M95 (≠ Q85), Y154 (≠ F144), R157 (= R147), E231 (= E215), K288 (= K272), G316 (= G300)
- binding pyridoxal-5'-phosphate: G127 (= G117), A128 (= A118), Y154 (≠ F144), H155 (= H145), D259 (= D243), V261 (= V245)
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)
35% identity, 90% coverage: 43:428/428 of query aligns to 66:463/474 of O58478
- D251 (≠ E215) mutation to A: Loss of activity.
- K308 (= K272) 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, 90% coverage: 33:419/428 of query aligns to 40:445/454 of O50131
- T92 (≠ Q85) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ V86) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G117) binding pyridoxal 5'-phosphate
- T125 (≠ A118) binding pyridoxal 5'-phosphate
- Q267 (= Q246) binding pyridoxal 5'-phosphate
- K293 (= K272) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T301) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
37% identity, 90% coverage: 33:419/428 of query aligns to 38:443/452 of 7vo1A