SitesBLAST
Comparing AO356_26715 AO356_26715 4-aminobutyrate aminotransferase 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)
51% identity, 98% coverage: 1:421/430 of query aligns to 1:417/426 of P22256
- I50 (= I54) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 115:116) binding
- E211 (≠ D215) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ I245) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q246) binding
- K268 (= K272) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T301) binding
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
51% identity, 96% coverage: 11:421/430 of query aligns to 6:416/425 of 1sffA
- active site: V18 (≠ L23), Y137 (≠ F142), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T301), R397 (= R402)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q83), G110 (= G115), S111 (≠ A116), Y137 (≠ F142), H138 (= H143), R140 (= R145), E205 (= E210), D238 (= D243), V240 (≠ I245), Q241 (= Q246), K267 (= K272), T296 (= T301)
- binding sulfate ion: N152 (≠ Q157), Y393 (≠ R398)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
51% identity, 96% coverage: 11:421/430 of query aligns to 6:416/425 of 1sf2A
- active site: V18 (≠ L23), Y137 (≠ F142), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T301), R397 (= R402)
- binding pyridoxal-5'-phosphate: G110 (= G115), S111 (≠ A116), Y137 (≠ F142), H138 (= H143), E205 (= E210), D238 (= D243), V240 (≠ I245), Q241 (= Q246), K267 (= K272)
- binding sulfate ion: N152 (≠ Q157), Y393 (≠ R398)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
51% identity, 96% coverage: 11:421/430 of query aligns to 6:416/425 of 1szkA
- active site: V18 (≠ L23), Y137 (≠ F142), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T301), R397 (= R402)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G115), S111 (≠ A116), Y137 (≠ F142), H138 (= H143), E205 (= E210), D238 (= D243), V240 (≠ I245), Q241 (= Q246), K267 (= K272)
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)
49% identity, 96% coverage: 13:425/430 of query aligns to 8:419/421 of P50457
- K267 (= K272) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
46% identity, 97% coverage: 11:428/430 of query aligns to 20:438/439 of 3q8nC
- active site: V32 (≠ L23), Y151 (≠ F142), E221 (= E210), D254 (= D243), Q257 (= Q246), K283 (= K272), T312 (= T301), R412 (= R402)
- binding 4-oxobutanoic acid: G124 (= G115), A125 (= A116), V256 (≠ I245), K283 (= K272)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
42% identity, 98% coverage: 7:427/430 of query aligns to 19:437/440 of 6j2vA
- active site: L35 (= L23), Y154 (≠ F142), D256 (= D243), K285 (= K272)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G115), A128 (= A116), Y154 (≠ F142), H155 (= H143), R157 (= R145), E223 (= E210), E228 (≠ D215), D256 (= D243), I258 (= I245), K285 (= K272), G313 (= G300), T314 (= T301)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
44% identity, 97% coverage: 7:425/430 of query aligns to 19:441/444 of 4atqF
- active site: V35 (≠ L23), Y154 (≠ F142), E226 (= E210), D259 (= D243), Q262 (= Q246), K288 (= K272), T317 (= T301), R418 (= R402)
- binding gamma-amino-butanoic acid: M95 (≠ Q83), Y154 (≠ F142), R157 (= R145), E231 (≠ D215), K288 (= K272), G316 (= G300)
- binding pyridoxal-5'-phosphate: G127 (= G115), A128 (= A116), Y154 (≠ F142), H155 (= H143), D259 (= D243), V261 (≠ I245)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
36% identity, 99% coverage: 4:428/430 of query aligns to 10:441/448 of 4ysnC
- active site: A29 (≠ L23), Y149 (≠ F142), E224 (= E210), D257 (= D243), N260 (≠ Q246), K287 (= K272), T316 (≠ G300), R415 (= R402)
- binding pyridoxal-5'-phosphate: S121 (= S114), G122 (= G115), S123 (≠ A116), Y149 (≠ F142), H150 (= H143), E224 (= E210), D257 (= D243), V259 (≠ I245), K287 (= K272), F315 (≠ G299), T316 (≠ G300)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
36% identity, 99% coverage: 4:428/430 of query aligns to 1:432/439 of 5wyaA
- active site: A20 (≠ L23), Y140 (≠ F142), E215 (= E210), D248 (= D243), N251 (≠ Q246), K278 (= K272), T307 (≠ G300), R406 (= R402)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I54), Y82 (≠ V84), S112 (= S114), G113 (= G115), S114 (≠ A116), Y140 (≠ F142), H141 (= H143), E215 (= E210), D248 (= D243), V250 (≠ I245), N251 (≠ Q246), K278 (= K272), F306 (≠ G299), T307 (≠ G300), R406 (= R402)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
36% identity, 99% coverage: 4:428/430 of query aligns to 3:434/446 of 5wyfA
- active site: A22 (≠ L23), Y142 (≠ F142), E217 (= E210), D250 (= D243), N253 (≠ Q246), K280 (= K272), T309 (≠ G300), R408 (= R402)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I54), Y84 (≠ V84), G115 (= G115), S116 (≠ A116), Y142 (≠ F142), H143 (= H143), D222 (= D215), D250 (= D243), V252 (≠ I245), N253 (≠ Q246), K280 (= K272), F308 (≠ G299), T309 (≠ G300), R408 (= R402)
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)
39% identity, 92% coverage: 29:425/430 of query aligns to 38:442/454 of O50131
- T92 (≠ V84) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ V85) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G115) binding
- T125 (≠ A116) binding
- Q267 (= Q246) binding
- K293 (= K272) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T301) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
39% identity, 92% coverage: 29:425/430 of query aligns to 36:440/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I54), S121 (= S114), G122 (= G115), T123 (≠ A116), F149 (= F142), H150 (= H143), R152 (= R145), E234 (≠ D215), D262 (= D243), V264 (≠ I245), Q265 (= Q246), K291 (= K272), N318 (≠ G300), T319 (= T301), R417 (= R402)
7vntA Structure of aminotransferase-substrate complex (see paper)
39% identity, 92% coverage: 29:425/430 of query aligns to 36:440/452 of 7vntA
- binding L-ornithine: F149 (= F142), R152 (= R145), E234 (≠ D215), K291 (= K272)
- binding pyridoxal-5'-phosphate: G122 (= G115), T123 (≠ A116), F149 (= F142), H150 (= H143), E229 (= E210), D262 (= D243), V264 (≠ I245), Q265 (= Q246), K291 (= K272)
7vnoA Structure of aminotransferase (see paper)
39% identity, 92% coverage: 29:425/430 of query aligns to 36:440/452 of 7vnoA
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)
33% identity, 97% coverage: 11:425/430 of query aligns to 35:458/474 of O58478
- D251 (= D215) mutation to A: Loss of activity.
- K308 (= K272) mutation to A: Loss of activity.
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
37% identity, 99% coverage: 1:425/430 of query aligns to 1:394/395 of Q5SHH5
- GT 113:114 (≠ GA 115:116) binding
- K254 (= K272) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T301) binding
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
37% identity, 96% coverage: 12:425/430 of query aligns to 4:386/387 of 1wkhA
- active site: S13 (≠ R21), F132 (= F142), E184 (= E210), D217 (= D243), Q220 (= Q246), K246 (= K272), T275 (= T301), R363 (= R402)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ I54), S104 (= S114), G105 (= G115), T106 (≠ A116), F132 (= F142), S133 (≠ H143), E184 (= E210), E189 (≠ D215), D217 (= D243), I219 (= I245), K246 (= K272), R363 (= R402)
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
37% identity, 96% coverage: 12:425/430 of query aligns to 4:386/387 of 1wkgA
- active site: S13 (≠ R21), F132 (= F142), E184 (= E210), D217 (= D243), Q220 (= Q246), K246 (= K272), T275 (= T301), R363 (= R402)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y16 (≠ V24), Y46 (≠ I54), G105 (= G115), T106 (≠ A116), F132 (= F142), S133 (≠ H143), R135 (= R145), E184 (= E210), D217 (= D243), I219 (= I245), Q220 (= Q246), K246 (= K272), G273 (= G299), T274 (≠ G300), T275 (= T301)
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
37% identity, 96% coverage: 12:425/430 of query aligns to 4:386/387 of 1vefA
- active site: S13 (≠ R21), F132 (= F142), D217 (= D243), K246 (= K272), T275 (= T301), R363 (= R402)
- binding pyridoxal-5'-phosphate: G105 (= G115), T106 (≠ A116), F132 (= F142), S133 (≠ H143), E184 (= E210), D217 (= D243), I219 (= I245), K246 (= K272)
Query Sequence
>AO356_26715 AO356_26715 4-aminobutyrate aminotransferase
MNSKVEETPSLLRQRDQFVPRGLVTAHPLVIDRAQGAEVWDVDGARYLDFVGGIGVLNIG
HNHPKVVAAVQAQLQKVSHACFQVVAYKPYLDLVKRLCELVGGQQAYKAALFTSGAEAVE
NAVKIARAHTNRPAVISFRGGFHGRTLLGTTLTGMSQPYKQNFGPFAPEVFHTPYPNAYR
GFSSEMALQALNELLATQVAPDRVAAIIIEPVQGDGGFLSAPPEFLQALRTLTEQHGIVL
ILDEIQTGFGRTGKWFGFQHAGIQPDLVTVAKSLAGGLPISGVVGRAHIMDAPLPGGLGG
TYGGNALSCAAALAVIDAYEQEQLLERGQVLGERLRQGLLRLQARHPRIGDVRGTGFMLA
IELIKDDEARSPDAELTQQLIDQARVGRLLVIKCGVHRNVLRFLAPLVTEESQIDEALTI
LEAALLRVLD
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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