SitesBLAST
Comparing GFF3586 FitnessBrowser__psRCH2:GFF3586 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)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
75% identity, 99% coverage: 3:424/426 of query aligns to 1:422/425 of 1sffA
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R399)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q80), G110 (= G112), S111 (= S113), Y137 (= Y139), H138 (= H140), R140 (= R142), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269), T296 (= T298)
- binding sulfate ion: N152 (≠ A154), Y393 (= Y395)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
75% identity, 99% coverage: 3:424/426 of query aligns to 1:422/425 of 1sf2A
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R399)
- binding pyridoxal-5'-phosphate: G110 (= G112), S111 (= S113), Y137 (= Y139), H138 (= H140), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269)
- binding sulfate ion: N152 (≠ A154), Y393 (= Y395)
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)
75% identity, 99% coverage: 3:424/426 of query aligns to 2:423/426 of P22256
- I50 (= I51) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 112:113) binding pyridoxal 5'-phosphate
- E211 (= E212) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V242) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q243) binding pyridoxal 5'-phosphate
- K268 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T298) binding pyridoxal 5'-phosphate
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
75% identity, 99% coverage: 3:424/426 of query aligns to 1:422/425 of 1szkA
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R399)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G112), S111 (= S113), Y137 (= Y139), H138 (= H140), E205 (= E207), D238 (= D240), V240 (= V242), Q241 (= Q243), K267 (= K269)
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)
54% identity, 99% coverage: 4:424/426 of query aligns to 2:421/421 of P50457
- K267 (= K269) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
45% identity, 99% coverage: 5:425/426 of query aligns to 17:438/439 of 3q8nC
- active site: V32 (= V20), Y151 (= Y139), E221 (= E207), D254 (= D240), Q257 (= Q243), K283 (= K269), T312 (= T298), R412 (= R399)
- binding 4-oxobutanoic acid: G124 (= G112), A125 (≠ S113), V256 (= V242), K283 (= K269)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
43% identity, 97% coverage: 5:418/426 of query aligns to 20:437/444 of 4atqF
- active site: V35 (= V20), Y154 (= Y139), E226 (= E207), D259 (= D240), Q262 (= Q243), K288 (= K269), T317 (= T298), R418 (= R399)
- binding gamma-amino-butanoic acid: M95 (≠ Q80), Y154 (= Y139), R157 (= R142), E231 (= E212), K288 (= K269), G316 (= G297)
- binding pyridoxal-5'-phosphate: G127 (= G112), A128 (≠ S113), Y154 (= Y139), H155 (= H140), D259 (= D240), V261 (= V242)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
43% identity, 97% coverage: 5:418/426 of query aligns to 20:431/440 of 6j2vA
- active site: L35 (≠ V20), Y154 (= Y139), D256 (= D240), K285 (= K269)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G112), A128 (≠ S113), Y154 (= Y139), H155 (= H140), R157 (= R142), E223 (= E207), E228 (= E212), D256 (= D240), I258 (≠ V242), K285 (= K269), G313 (= G297), T314 (= T298)
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, 99% coverage: 6:426/426 of query aligns to 33:463/474 of O58478
- D251 (≠ E212) mutation to A: Loss of activity.
- K308 (= K269) 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, 92% coverage: 29:421/426 of query aligns to 41:441/454 of O50131
- T92 (≠ V81) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ L82) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G112) binding pyridoxal 5'-phosphate
- T125 (≠ S113) binding pyridoxal 5'-phosphate
- Q267 (= Q243) binding pyridoxal 5'-phosphate
- K293 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T298) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
37% identity, 92% coverage: 29:421/426 of query aligns to 39:439/452 of 7vo1A