SitesBLAST
Comparing WP_012172510.1 NCBI__GCF_000010525.1:WP_012172510.1 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)
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)
31% identity, 94% coverage: 22:466/475 of query aligns to 31:455/474 of O58478
- D251 (≠ T247) mutation to A: Loss of activity.
- K308 (= K304) mutation to A: Loss of activity.
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
31% identity, 89% coverage: 45:465/475 of query aligns to 23:416/425 of 1szkA
- active site: Y137 (= Y161), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T336), R397 (≠ T446)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G133), S111 (= S134), Y137 (= Y161), H138 (= H162), E205 (= E242), D238 (= D275), V240 (≠ I277), Q241 (= Q278), K267 (= K304)
Sites not aligning to the query:
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)
32% identity, 90% coverage: 47:473/475 of query aligns to 39:446/454 of O50131
- T92 (≠ S99) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ Q100) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G133) binding pyridoxal 5'-phosphate
- T125 (≠ S134) binding pyridoxal 5'-phosphate
- Q267 (= Q278) binding pyridoxal 5'-phosphate
- K293 (= K304) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T336) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
32% identity, 90% coverage: 47:473/475 of query aligns to 37:444/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ Y71), S121 (≠ G132), G122 (= G133), T123 (≠ S134), F149 (≠ Y161), H150 (= H162), R152 (= R164), E234 (≠ T247), D262 (= D275), V264 (≠ I277), Q265 (= Q278), K291 (= K304), N318 (vs. gap), T319 (= T336), R417 (≠ T446)
7vntA Structure of aminotransferase-substrate complex (see paper)
32% identity, 90% coverage: 47:473/475 of query aligns to 37:444/452 of 7vntA
- binding L-ornithine: F149 (≠ Y161), R152 (= R164), E234 (≠ T247), K291 (= K304)
- binding pyridoxal-5'-phosphate: G122 (= G133), T123 (≠ S134), F149 (≠ Y161), H150 (= H162), E229 (= E242), D262 (= D275), V264 (≠ I277), Q265 (= Q278), K291 (= K304)
7vnoA Structure of aminotransferase (see paper)
32% identity, 90% coverage: 47:473/475 of query aligns to 37:444/452 of 7vnoA
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
31% identity, 89% coverage: 45:465/475 of query aligns to 23:416/425 of 1sffA
- active site: Y137 (= Y161), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T336), R397 (≠ T446)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q100), G110 (= G133), S111 (= S134), Y137 (= Y161), H138 (= H162), R140 (= R164), E205 (= E242), D238 (= D275), V240 (≠ I277), Q241 (= Q278), K267 (= K304), T296 (= T336)
- binding sulfate ion: N152 (vs. gap), Y393 (≠ K442)
Sites not aligning to the query:
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
31% identity, 89% coverage: 45:465/475 of query aligns to 23:416/425 of 1sf2A
- active site: Y137 (= Y161), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T336), R397 (≠ T446)
- binding pyridoxal-5'-phosphate: G110 (= G133), S111 (= S134), Y137 (= Y161), H138 (= H162), E205 (= E242), D238 (= D275), V240 (≠ I277), Q241 (= Q278), K267 (= K304)
- binding sulfate ion: N152 (vs. gap), Y393 (≠ K442)
Sites not aligning to the query:
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)
31% identity, 89% coverage: 45:465/475 of query aligns to 24:417/426 of P22256
- I50 (≠ Y71) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 133:134) binding pyridoxal 5'-phosphate
- E211 (≠ T247) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I277) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q278) binding pyridoxal 5'-phosphate
- K268 (= K304) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T336) binding pyridoxal 5'-phosphate
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
31% identity, 90% coverage: 45:472/475 of query aligns to 25:412/412 of 2eo5A
- active site: F139 (≠ Y161), E219 (= E242), D252 (= D275), Q255 (= Q278), K281 (= K304), T303 (= T336), R386 (≠ T446)
- binding pyridoxal-5'-phosphate: G113 (= G133), T114 (≠ S134), F139 (≠ Y161), H140 (= H162), E219 (= E242), D252 (= D275), V254 (≠ I277), Q255 (= Q278), K281 (= K304)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
28% identity, 96% coverage: 20:475/475 of query aligns to 11:444/448 of 4ysnC