SitesBLAST
Comparing 200454 FitnessBrowser__MR1:200454 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
70% identity, 98% coverage: 3:420/425 of query aligns to 1:421/425 of 1sffA
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R396)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ M80), 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 (≠ G392)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
70% identity, 98% coverage: 3:420/425 of query aligns to 1:421/425 of 1sf2A
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R396)
- 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 (≠ G392)
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)
70% identity, 98% coverage: 3:420/425 of query aligns to 2:422/426 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)
70% identity, 98% coverage: 3:420/425 of query aligns to 1:421/425 of 1szkA
- active site: V18 (= V20), Y137 (= Y139), E205 (= E207), D238 (= D240), Q241 (= Q243), K267 (= K269), T296 (= T298), R397 (= R396)
- 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)
52% identity, 98% coverage: 4:420/425 of query aligns to 2:420/421 of P50457
- K267 (= K269) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
47% identity, 98% coverage: 5:422/425 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 (= R396)
- binding 4-oxobutanoic acid: G124 (= G112), A125 (≠ S113), V256 (= V242), K283 (= K269)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
46% identity, 97% coverage: 5:415/425 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)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
46% identity, 98% coverage: 5:421/425 of query aligns to 20:443/444 of 4atqF
- active site: V35 (= V20), Y154 (= Y139), E226 (= E207), D259 (= D240), Q262 (= Q243), K288 (= K269), T317 (= T298), R418 (= R396)
- binding gamma-amino-butanoic acid: M95 (= M80), 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)
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, 99% coverage: 7:425/425 of query aligns to 34:464/474 of O58478
- D251 (≠ E212) mutation to A: Loss of activity.
- K308 (= K269) mutation to A: Loss of activity.
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
32% identity, 93% coverage: 30:425/425 of query aligns to 33:437/446 of 5wyfA
- active site: Y142 (= Y139), E217 (= E207), D250 (= D240), N253 (≠ Q243), K280 (= K269), T309 (= T298), R408 (= R396)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I51), Y84 (≠ V81), G115 (= G112), S116 (= S113), Y142 (= Y139), H143 (= H140), D222 (≠ E212), D250 (= D240), V252 (= V242), N253 (≠ Q243), K280 (= K269), F308 (≠ G297), T309 (= T298), R408 (= R396)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
32% identity, 93% coverage: 30:425/425 of query aligns to 31:435/439 of 5wyaA