SitesBLAST
Comparing Ac3H11_4179 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19) 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)
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)
62% identity, 92% coverage: 33:452/459 of query aligns to 3:422/426 of P22256
- I50 (= I80) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 141:142) binding
- E211 (= E241) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V271) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q272) binding
- K268 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T327) binding
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
62% identity, 92% coverage: 33:452/459 of query aligns to 2:421/425 of 1sffA
- active site: V18 (= V49), Y137 (= Y168), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R428)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q109), G110 (= G141), S111 (≠ A142), Y137 (= Y168), H138 (= H169), R140 (= R171), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (= Q272), K267 (= K298), T296 (= T327)
- binding sulfate ion: N152 (≠ A183), Y393 (≠ G424)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
62% identity, 92% coverage: 33:452/459 of query aligns to 2:421/425 of 1sf2A
- active site: V18 (= V49), Y137 (= Y168), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R428)
- binding pyridoxal-5'-phosphate: G110 (= G141), S111 (≠ A142), Y137 (= Y168), H138 (= H169), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (= Q272), K267 (= K298)
- binding sulfate ion: N152 (≠ A183), Y393 (≠ G424)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
61% identity, 92% coverage: 33:452/459 of query aligns to 2:421/425 of 1szkA
- active site: V18 (= V49), Y137 (= Y168), E205 (= E236), D238 (= D269), Q241 (= Q272), K267 (= K298), T296 (= T327), R397 (= R428)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G141), S111 (≠ A142), Y137 (= Y168), H138 (= H169), E205 (= E236), D238 (= D269), V240 (= V271), Q241 (= Q272), K267 (= K298)
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, 92% coverage: 32:451/459 of query aligns to 1:419/421 of P50457
- K267 (= K298) mutation to A: No GABA-AT activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
48% identity, 92% coverage: 25:448/459 of query aligns to 1:432/439 of 3q8nC
- active site: V32 (= V49), Y151 (= Y168), E221 (= E236), D254 (= D269), Q257 (= Q272), K283 (= K298), T312 (= T327), R412 (= R428)
- binding 4-oxobutanoic acid: G124 (= G141), A125 (= A142), V256 (= V271), K283 (= K298)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
47% identity, 93% coverage: 24:452/459 of query aligns to 10:436/440 of 6j2vA
- active site: L35 (≠ V49), Y154 (= Y168), D256 (= D269), K285 (= K298)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G141), A128 (= A142), Y154 (= Y168), H155 (= H169), R157 (= R171), E223 (= E236), E228 (= E241), D256 (= D269), I258 (≠ V271), K285 (= K298), G313 (= G326), T314 (= T327)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
47% identity, 93% coverage: 26:453/459 of query aligns to 5:443/444 of 4atqF
- active site: V35 (= V49), Y154 (= Y168), E226 (= E236), D259 (= D269), Q262 (= Q272), K288 (= K298), T317 (= T327), R418 (= R428)
- binding gamma-amino-butanoic acid: M95 (≠ Q109), Y154 (= Y168), R157 (= R171), E231 (= E241), K288 (= K298), G316 (= G326)
- binding pyridoxal-5'-phosphate: G127 (= G141), A128 (= A142), Y154 (= Y168), H155 (= H169), D259 (= D269), V261 (= V271)
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, 92% coverage: 37:456/459 of query aligns to 35:463/474 of O58478
- D251 (≠ E241) mutation to A: Loss of activity.
- K308 (= K298) 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, 91% coverage: 37:455/459 of query aligns to 18:446/454 of O50131
- T92 (≠ V110) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ V111) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G141) binding
- T125 (≠ A142) binding
- Q267 (= Q272) binding
- K293 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T327) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
37% identity, 91% coverage: 37:455/459 of query aligns to 16:444/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I80), S121 (≠ T140), G122 (= G141), T123 (≠ A142), F149 (≠ Y168), H150 (= H169), R152 (= R171), E234 (= E241), D262 (= D269), V264 (= V271), Q265 (= Q272), K291 (= K298), N318 (≠ G326), T319 (= T327), R417 (= R428)
7vntA Structure of aminotransferase-substrate complex (see paper)
37% identity, 91% coverage: 37:455/459 of query aligns to 16:444/452 of 7vntA
- binding L-ornithine: F149 (≠ Y168), R152 (= R171), E234 (= E241), K291 (= K298)
- binding pyridoxal-5'-phosphate: G122 (= G141), T123 (≠ A142), F149 (≠ Y168), H150 (= H169), E229 (= E236), D262 (= D269), V264 (= V271), Q265 (= Q272), K291 (= K298)
7vnoA Structure of aminotransferase (see paper)
37% identity, 91% coverage: 37:455/459 of query aligns to 16:444/452 of 7vnoA
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 88% coverage: 53:454/459 of query aligns to 34:441/448 of 4ysnC
- active site: Y149 (= Y168), E224 (= E236), D257 (= D269), N260 (≠ Q272), K287 (= K298), T316 (≠ G326), R415 (= R428)
- binding pyridoxal-5'-phosphate: S121 (≠ T140), G122 (= G141), S123 (≠ A142), Y149 (= Y168), H150 (= H169), E224 (= E236), D257 (= D269), V259 (= V271), K287 (= K298), F315 (≠ G325), T316 (≠ G326)
Sites not aligning to the query:
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
33% identity, 88% coverage: 53:454/459 of query aligns to 25:432/439 of 5wyaA
- active site: Y140 (= Y168), E215 (= E236), D248 (= D269), N251 (≠ Q272), K278 (= K298), T307 (≠ G326), R406 (= R428)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I80), Y82 (≠ V110), S112 (≠ T140), G113 (= G141), S114 (≠ A142), Y140 (= Y168), H141 (= H169), E215 (= E236), D248 (= D269), V250 (= V271), N251 (≠ Q272), K278 (= K298), F306 (≠ G325), T307 (≠ G326), R406 (= R428)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
33% identity, 88% coverage: 53:454/459 of query aligns to 27:434/446 of 5wyfA
- active site: Y142 (= Y168), E217 (= E236), D250 (= D269), N253 (≠ Q272), K280 (= K298), T309 (≠ G326), R408 (= R428)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I80), Y84 (≠ V110), G115 (= G141), S116 (≠ A142), Y142 (= Y168), H143 (= H169), D222 (≠ E241), D250 (= D269), V252 (= V271), N253 (≠ Q272), K280 (= K298), F308 (≠ G325), T309 (≠ G326), R408 (= R428)
Sites not aligning to the query:
P40732 Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
32% identity, 87% coverage: 54:454/459 of query aligns to 25:403/405 of P40732
- GT 108:109 (≠ GA 141:142) binding
- K255 (= K298) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T327) binding
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
32% identity, 87% coverage: 54:454/459 of query aligns to 20:398/402 of 4jevB
- active site: F136 (≠ Y168), E188 (= E236), D221 (= D269), Q224 (= Q272), K250 (= K298), T279 (= T327), R372 (= R428)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I80), S102 (≠ T140), G103 (= G141), T104 (≠ A142), F136 (≠ Y168), H137 (= H169), E188 (= E236), E193 (= E241), D221 (= D269), V223 (= V271), Q224 (= Q272), K250 (= K298), R372 (= R428)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
32% identity, 87% coverage: 54:454/459 of query aligns to 20:393/397 of 4jewA
- active site: F136 (≠ Y168), E188 (= E236), D221 (= D269), Q224 (= Q272), K250 (= K298), T274 (= T327), R367 (= R428)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G141), T104 (≠ A142), F136 (≠ Y168), H137 (= H169), R139 (= R171), E188 (= E236), E193 (= E241), D221 (= D269), V223 (= V271), K250 (= K298)
- binding picric acid: K25 (= K59), K27 (≠ R61), W32 (= W66)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
32% identity, 87% coverage: 54:454/459 of query aligns to 14:387/389 of 2pb0A
- active site: F130 (≠ Y168), E182 (= E236), D215 (= D269), Q218 (= Q272), K244 (= K298), T268 (= T327), R361 (= R428)
- binding pyridoxal-5'-phosphate: S96 (≠ T140), G97 (= G141), T98 (≠ A142), F130 (≠ Y168), H131 (= H169), E182 (= E236), D215 (= D269), V217 (= V271), Q218 (= Q272), K244 (= K298)
Query Sequence
>Ac3H11_4179 Gamma-aminobutyrate:alpha-ketoglutarate aminotransferase (EC 2.6.1.19)
MDGVWRDFQNPPHSFISSSTTTPTTMQQDRHFTNAALLTRRHAAVARGVGQAHDLFIQKA
RNAELWDVEGRRFIDFAGGIAVLNTGHLHAGVIAAVKAQLDLYTHTCFQVVAYEPYVEVC
ERLNTLAPGAFAKKSLLLTTGAEAVENAIKIARAYTKRPGVIAFTGGYHGRTNLTLGLTG
KVAPYKIGFGPFPGETYHALFPNALHGVSVEQALHSVELIFKNDIEPERVAAFIVEPVQG
EGGFYVAPPEFISGLKTLADRYGILLIADEVQTGAGRTGTWFASEQWPVAPDLITTAKSL
AGGFPLAGVVGRADVMDAPAPGGLGGTYAGSPVACAASLAVIEAFAQEKLLARSQDMGAL
LVRSLKDLAARIPAIGDVRGLGAMVAIELFENGDLSRPDAALTKQVVAEAARRGLILLSC
GTHGNVIRILVPLTASDELLHEGLAILADSLEAVATAAN
Or try a new SitesBLAST search
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