SitesBLAST
Comparing 6938533 FitnessBrowser__SB2B:6938533 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)
68% identity, 98% coverage: 4:420/425 of query aligns to 3:422/426 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
- 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
- K268 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T298) binding
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
68% identity, 98% coverage: 4:420/425 of query aligns to 2:421/425 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)
68% identity, 98% coverage: 4:420/425 of query aligns to 2:421/425 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)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
68% identity, 98% coverage: 4:420/425 of query aligns to 2:421/425 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)
51% identity, 98% coverage: 3:419/425 of query aligns to 1:419/421 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)
45% identity, 96% coverage: 11:420/425 of query aligns to 26:436/440 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)
36% identity, 98% coverage: 8:423/425 of query aligns to 35:462/474 of O58478
- D251 (≠ E212) mutation to A: Loss of activity.
- K308 (= K269) mutation to A: Loss of activity.
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 93% coverage: 29:422/425 of query aligns to 39:441/448 of 4ysnC
- active site: Y149 (= Y139), E224 (= E207), D257 (= D240), N260 (≠ Q243), K287 (= K269), T316 (= T298), R415 (= R396)
- binding pyridoxal-5'-phosphate: S121 (= S111), G122 (= G112), S123 (= S113), Y149 (= Y139), H150 (= H140), E224 (= E207), D257 (= D240), V259 (= V242), K287 (= K269), F315 (≠ G297), T316 (= T298)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 93% coverage: 29:422/425 of query aligns to 30:432/439 of 5wyaA
- active site: Y140 (= Y139), E215 (= E207), D248 (= D240), N251 (≠ Q243), K278 (= K269), T307 (= T298), R406 (= R396)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I51), Y82 (≠ V81), S112 (= S111), G113 (= G112), S114 (= S113), Y140 (= Y139), H141 (= H140), E215 (= E207), D248 (= D240), V250 (= V242), N251 (≠ Q243), K278 (= K269), F306 (≠ G297), T307 (= T298), R406 (= R396)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 93% coverage: 29:422/425 of query aligns to 32:434/446 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:
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
35% identity, 94% coverage: 25:425/425 of query aligns to 20:401/401 of 4adbB
- active site: F136 (≠ Y139), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T298), R372 (= R396)
- binding pyridoxal-5'-phosphate: S102 (= S111), G103 (= G112), A104 (≠ S113), F136 (≠ Y139), H137 (= H140), D221 (= D240), V223 (= V242), Q224 (= Q243), K250 (= K269)
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
35% identity, 93% coverage: 25:420/425 of query aligns to 20:396/400 of 4addA
- active site: F136 (≠ Y139), E188 (= E207), D221 (= D240), Q224 (= Q243), K250 (= K269), T279 (= T298), R372 (= R396)
- binding pyridoxal-5'-phosphate: G103 (= G112), A104 (≠ S113), F136 (≠ Y139), H137 (= H140), D221 (= D240), V223 (= V242), K250 (= K269)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: F136 (≠ Y139), R139 (= R142)
Sites not aligning to the query:
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 93% coverage: 19:413/425 of query aligns to 22:388/395 of Q5SHH5
- GT 113:114 (≠ GS 112:113) binding
- K254 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T298) binding
2eh6A Crystal structure of acetylornithine aminotransferase from aquifex aeolicus vf5
35% identity, 93% coverage: 25:419/425 of query aligns to 11:375/375 of 2eh6A
- active site: F127 (≠ Y139), E179 (= E207), D212 (= D240), Q215 (= Q243), K241 (= K269), T270 (= T298), R352 (= R396)
- binding pyridoxal-5'-phosphate: G95 (= G112), T96 (≠ S113), F127 (≠ Y139), H128 (= H140), E179 (= E207), D212 (= D240), V214 (= V242), K241 (= K269)
O66442 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Aquifex aeolicus (strain VF5)
35% identity, 93% coverage: 25:419/425 of query aligns to 12:376/376 of O66442
- GT 96:97 (≠ GS 112:113) binding
- K242 (= K269) modified: N6-(pyridoxal phosphate)lysine
- T271 (= T298) binding
Q9M8M7 Acetylornithine aminotransferase, chloroplastic/mitochondrial; ACOAT; Acetylornithine transaminase; AOTA; Protein HOPW1-1-INTERACTING 1; EC 2.6.1.11 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 97% coverage: 9:422/425 of query aligns to 61:456/457 of Q9M8M7
Sites not aligning to the query:
- 1:41 modified: transit peptide, Chloroplast and mitochondrion
- 42 modified: N-acetylvaline; in Acetylornithine aminotransferase, chloroplastic
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 93% coverage: 19:413/425 of query aligns to 14:380/387 of 1wkhA
- active site: F132 (≠ Y139), E184 (= E207), D217 (= D240), Q220 (= Q243), K246 (= K269), T275 (= T298), R363 (= R396)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I51), S104 (= S111), G105 (= G112), T106 (≠ S113), F132 (≠ Y139), S133 (≠ H140), E184 (= E207), E189 (= E212), D217 (= D240), I219 (≠ V242), K246 (= K269), R363 (= R396)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
36% identity, 93% coverage: 19:413/425 of query aligns to 14:380/387 of 1wkgA
- active site: F132 (≠ Y139), E184 (= E207), D217 (= D240), Q220 (= Q243), K246 (= K269), T275 (= T298), R363 (= R396)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (≠ G21), Y46 (≠ I51), G105 (= G112), T106 (≠ S113), F132 (≠ Y139), S133 (≠ H140), R135 (= R142), E184 (= E207), D217 (= D240), I219 (≠ V242), Q220 (= Q243), K246 (= K269), G273 (= G296), T274 (≠ G297), T275 (= T298)
Sites not aligning to the query:
Query Sequence
>6938533 FitnessBrowser__SB2B:6938533
MSLTNDSLMVRRRAAVAGGVGQIHPVFTERAENATVWDVEGREYIDFAGGIAVLNTGHLH
PKVKAAVAEQLEKFSHTCFMVLGYESYVAVCEKLNQLVPGDFAKKSALFTSGSEAVENAI
KVARAYTKRAGVIAFTSGYHGRTMAALALTGKVAPYSKGMGLMQANVFRAEFPCALHGVS
EDDAMASIERIFKNDAEPSDIAAIILEPVQGEGGFYAATPGFMKRLRELCDREGIMLIAD
EVQTGAGRTGTFFAMEQMGVAADITTFAKSIAGGFPLSGITGRAEVMDAIGPGGLGGTYG
GSPLACAAALAVIEVFEEEKLLERSNAIGQTIKSAIGELASRYPQIAEVRGLGSMIAIEL
MENGKPAPEYCPQVLTEARNRGLILLSCGTYGNVLRILVPITAPDEQIQRGLEIMAECFE
AVLGK
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory