SitesBLAST
Comparing WP_011022811.1 NCBI__GCF_000007345.1:WP_011022811.1 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)
7vo1A Structure of aminotransferase-substrate complex (see paper)
45% identity, 89% coverage: 51:473/477 of query aligns to 7:441/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I103), S121 (= S160), G122 (= G161), T123 (= T162), F149 (= F188), H150 (= H189), R152 (= R191), E234 (= E267), D262 (= D295), V264 (= V297), Q265 (= Q298), K291 (= K324), N318 (= N351), T319 (= T352), R417 (= R449)
7vntA Structure of aminotransferase-substrate complex (see paper)
45% identity, 89% coverage: 51:473/477 of query aligns to 7:441/452 of 7vntA
- binding L-ornithine: F149 (= F188), R152 (= R191), E234 (= E267), K291 (= K324)
- binding pyridoxal-5'-phosphate: G122 (= G161), T123 (= T162), F149 (= F188), H150 (= H189), E229 (= E262), D262 (= D295), V264 (= V297), Q265 (= Q298), K291 (= K324)
7vnoA Structure of aminotransferase (see paper)
45% identity, 89% coverage: 51:473/477 of query aligns to 7:441/452 of 7vnoA
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)
45% identity, 89% coverage: 51:473/477 of query aligns to 9:443/454 of O50131
- T92 (≠ G132) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D133) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G161) binding pyridoxal 5'-phosphate
- T125 (= T162) binding pyridoxal 5'-phosphate
- Q267 (= Q298) binding pyridoxal 5'-phosphate
- K293 (= K324) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T352) binding pyridoxal 5'-phosphate
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, 88% coverage: 54:473/477 of query aligns to 29:459/474 of O58478
- D251 (≠ E267) mutation to A: Loss of activity.
- K308 (= K324) mutation to A: Loss of activity.
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
40% identity, 87% coverage: 57:473/477 of query aligns to 3:410/412 of 2eo5A
- active site: T18 (≠ V72), F139 (= F188), E219 (= E262), D252 (= D295), Q255 (= Q298), K281 (= K324), T303 (= T352), R386 (= R449)
- binding pyridoxal-5'-phosphate: G113 (= G161), T114 (= T162), F139 (= F188), H140 (= H189), E219 (= E262), D252 (= D295), V254 (= V297), Q255 (= Q298), K281 (= K324)
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)
35% identity, 88% coverage: 58:477/477 of query aligns to 5:426/426 of P22256
- I50 (= I103) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 161:162) binding pyridoxal 5'-phosphate
- E211 (= E267) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V297) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q298) binding pyridoxal 5'-phosphate
- K268 (= K324) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T352) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
35% identity, 88% coverage: 58:477/477 of query aligns to 4:425/425 of 1sffA
- active site: V18 (= V72), Y137 (≠ F188), E205 (= E262), D238 (= D295), Q241 (= Q298), K267 (= K324), T296 (= T352), R397 (= R449)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ G132), G110 (= G161), S111 (≠ T162), Y137 (≠ F188), H138 (= H189), R140 (= R191), E205 (= E262), D238 (= D295), V240 (= V297), Q241 (= Q298), K267 (= K324), T296 (= T352)
- binding sulfate ion: N152 (≠ R204), Y393 (vs. gap)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
35% identity, 88% coverage: 58:477/477 of query aligns to 4:425/425 of 1sf2A
- active site: V18 (= V72), Y137 (≠ F188), E205 (= E262), D238 (= D295), Q241 (= Q298), K267 (= K324), T296 (= T352), R397 (= R449)
- binding pyridoxal-5'-phosphate: G110 (= G161), S111 (≠ T162), Y137 (≠ F188), H138 (= H189), E205 (= E262), D238 (= D295), V240 (= V297), Q241 (= Q298), K267 (= K324)
- binding sulfate ion: N152 (≠ R204), Y393 (vs. gap)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
35% identity, 88% coverage: 58:477/477 of query aligns to 4:425/425 of 1szkA
- active site: V18 (= V72), Y137 (≠ F188), E205 (= E262), D238 (= D295), Q241 (= Q298), K267 (= K324), T296 (= T352), R397 (= R449)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G161), S111 (≠ T162), Y137 (≠ F188), H138 (= H189), E205 (= E262), D238 (= D295), V240 (= V297), Q241 (= Q298), K267 (= K324)
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)
36% identity, 82% coverage: 83:472/477 of query aligns to 29:419/421 of P50457