SitesBLAST
Comparing WP_043527315.1 NCBI__GCF_000759345.1:WP_043527315.1 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)
49% identity, 97% coverage: 2:422/432 of query aligns to 3:423/426 of P22256
- I50 (= I49) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 110:111) binding pyridoxal 5'-phosphate
- E211 (= E210) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V240) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q241) binding pyridoxal 5'-phosphate
- K268 (= K267) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T296) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
49% identity, 97% coverage: 2:422/432 of query aligns to 2:422/425 of 1sffA
- active site: V18 (≠ A18), Y137 (= Y137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R397)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ T78), G110 (= G110), S111 (≠ A111), Y137 (= Y137), H138 (= H138), R140 (= R140), E205 (= E205), D238 (= D238), V240 (= V240), Q241 (= Q241), K267 (= K267), T296 (= T296)
- binding sulfate ion: N152 (≠ A152), Y393 (≠ G393)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
49% identity, 97% coverage: 2:422/432 of query aligns to 2:422/425 of 1sf2A
- active site: V18 (≠ A18), Y137 (= Y137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R397)
- binding pyridoxal-5'-phosphate: G110 (= G110), S111 (≠ A111), Y137 (= Y137), H138 (= H138), E205 (= E205), D238 (= D238), V240 (= V240), Q241 (= Q241), K267 (= K267)
- binding sulfate ion: N152 (≠ A152), Y393 (≠ G393)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
49% identity, 97% coverage: 2:422/432 of query aligns to 2:422/425 of 1szkA
- active site: V18 (≠ A18), Y137 (= Y137), E205 (= E205), D238 (= D238), Q241 (= Q241), K267 (= K267), T296 (= T296), R397 (= R397)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G110), S111 (≠ A111), Y137 (= Y137), H138 (= H138), E205 (= E205), D238 (= D238), V240 (= V240), Q241 (= Q241), K267 (= K267)
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)
46% identity, 98% coverage: 1:422/432 of query aligns to 1:421/421 of P50457
- K267 (= K267) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
42% identity, 97% coverage: 5:423/432 of query aligns to 19:438/439 of 3q8nC
- active site: V32 (≠ A18), Y151 (= Y137), E221 (= E205), D254 (= D238), Q257 (= Q241), K283 (= K267), T312 (= T296), R412 (= R397)
- binding 4-oxobutanoic acid: G124 (= G110), A125 (= A111), V256 (= V240), K283 (= K267)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
44% identity, 97% coverage: 6:422/432 of query aligns to 23:437/440 of 6j2vA
- active site: L35 (≠ A18), Y154 (= Y137), D256 (= D238), K285 (= K267)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G110), A128 (= A111), Y154 (= Y137), H155 (= H138), R157 (= R140), E223 (= E205), E228 (= E210), D256 (= D238), I258 (≠ V240), K285 (= K267), G313 (= G295), T314 (= T296)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
41% identity, 96% coverage: 6:421/432 of query aligns to 23:442/444 of 4atqF
- active site: V35 (≠ A18), Y154 (= Y137), E226 (= E205), D259 (= D238), Q262 (= Q241), K288 (= K267), T317 (= T296), R418 (= R397)
- binding gamma-amino-butanoic acid: M95 (≠ T78), Y154 (= Y137), R157 (= R140), E231 (= E210), K288 (= K267), G316 (= G295)
- binding pyridoxal-5'-phosphate: G127 (= G110), A128 (= A111), Y154 (= Y137), H155 (= H138), D259 (= D238), V261 (= V240)
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)
34% identity, 93% coverage: 28:428/432 of query aligns to 58:466/474 of O58478
- D251 (≠ E210) mutation to A: Loss of activity.
- K308 (= K267) 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, 96% coverage: 8:421/432 of query aligns to 20:443/454 of O50131
- T92 (= T78) 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 (= G110) binding pyridoxal 5'-phosphate
- T125 (≠ A111) binding pyridoxal 5'-phosphate
- Q267 (= Q241) binding pyridoxal 5'-phosphate
- K293 (= K267) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T296) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
37% identity, 96% coverage: 8:421/432 of query aligns to 18:441/452 of 7vo1A