SitesBLAST
Comparing HSERO_RS05420 HSERO_RS05420 4-aminobutyrate aminotransferase 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)
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)
69% identity, 98% coverage: 6:423/426 of query aligns to 2:419/421 of P50457
- K267 (= K271) mutation to A: No GABA-AT activity.
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)
55% identity, 98% coverage: 6:422/426 of query aligns to 3:420/426 of P22256
- I50 (= I53) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 114:115) binding
- E211 (= E214) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V244) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q245) binding
- K268 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T300) binding
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
55% identity, 98% coverage: 6:422/426 of query aligns to 2:419/425 of 1sffA
- active site: V18 (= V22), Y137 (≠ F141), E205 (= E209), D238 (= D242), Q241 (= Q245), K267 (= K271), T296 (= T300), R397 (= R400)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (= Q82), G110 (= G114), S111 (≠ A115), Y137 (≠ F141), H138 (= H142), R140 (= R144), E205 (= E209), D238 (= D242), V240 (= V244), Q241 (= Q245), K267 (= K271), T296 (= T300)
- binding sulfate ion: N152 (≠ A156), Y393 (≠ G396)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
55% identity, 98% coverage: 6:422/426 of query aligns to 2:419/425 of 1sf2A
- active site: V18 (= V22), Y137 (≠ F141), E205 (= E209), D238 (= D242), Q241 (= Q245), K267 (= K271), T296 (= T300), R397 (= R400)
- binding pyridoxal-5'-phosphate: G110 (= G114), S111 (≠ A115), Y137 (≠ F141), H138 (= H142), E205 (= E209), D238 (= D242), V240 (= V244), Q241 (= Q245), K267 (= K271)
- binding sulfate ion: N152 (≠ A156), Y393 (≠ G396)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
55% identity, 98% coverage: 6:422/426 of query aligns to 2:419/425 of 1szkA
- active site: V18 (= V22), Y137 (≠ F141), E205 (= E209), D238 (= D242), Q241 (= Q245), K267 (= K271), T296 (= T300), R397 (= R400)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G114), S111 (≠ A115), Y137 (≠ F141), H138 (= H142), E205 (= E209), D238 (= D242), V240 (= V244), Q241 (= Q245), K267 (= K271)
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
50% identity, 97% coverage: 7:420/426 of query aligns to 17:432/439 of 3q8nC
- active site: V32 (= V22), Y151 (≠ F141), E221 (= E209), D254 (= D242), Q257 (= Q245), K283 (= K271), T312 (= T300), R412 (= R400)
- binding 4-oxobutanoic acid: G124 (= G114), A125 (= A115), V256 (= V244), K283 (= K271)
6j2vA Gaba aminotransferase from corynebacterium glutamicum (see paper)
46% identity, 98% coverage: 6:423/426 of query aligns to 19:435/440 of 6j2vA
- active site: L35 (≠ V22), Y154 (≠ F141), D256 (= D242), K285 (= K271)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]butanoic acid: G127 (= G114), A128 (= A115), Y154 (≠ F141), H155 (= H142), R157 (= R144), E223 (= E209), E228 (= E214), D256 (= D242), I258 (≠ V244), K285 (= K271), G313 (= G299), T314 (= T300)
4atqF Gaba-transaminase a1r958 in complex with external aldimine plp-gaba adduct (see paper)
45% identity, 98% coverage: 6:424/426 of query aligns to 19:442/444 of 4atqF
- active site: V35 (= V22), Y154 (≠ F141), E226 (= E209), D259 (= D242), Q262 (= Q245), K288 (= K271), T317 (= T300), R418 (= R400)
- binding gamma-amino-butanoic acid: M95 (≠ Q82), Y154 (≠ F141), R157 (= R144), E231 (= E214), K288 (= K271), G316 (= G299)
- binding pyridoxal-5'-phosphate: G127 (= G114), A128 (= A115), Y154 (≠ F141), H155 (= H142), D259 (= D242), V261 (= V244)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
37% identity, 92% coverage: 31:423/426 of query aligns to 30:429/439 of 5wyaA
- active site: Y140 (≠ F141), E215 (= E209), D248 (= D242), N251 (≠ Q245), K278 (= K271), T307 (≠ G299), R406 (= R400)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ I53), Y82 (≠ I83), S112 (≠ T113), G113 (= G114), S114 (≠ A115), Y140 (≠ F141), H141 (= H142), E215 (= E209), D248 (= D242), V250 (= V244), N251 (≠ Q245), K278 (= K271), F306 (≠ G298), T307 (≠ G299), R406 (= R400)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
37% identity, 92% coverage: 31:423/426 of query aligns to 39:438/448 of 4ysnC
- active site: Y149 (≠ F141), E224 (= E209), D257 (= D242), N260 (≠ Q245), K287 (= K271), T316 (≠ G299), R415 (= R400)
- binding pyridoxal-5'-phosphate: S121 (≠ T113), G122 (= G114), S123 (≠ A115), Y149 (≠ F141), H150 (= H142), E224 (= E209), D257 (= D242), V259 (= V244), K287 (= K271), F315 (≠ G298), T316 (≠ G299)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
37% identity, 92% coverage: 31:423/426 of query aligns to 32:431/446 of 5wyfA
- active site: Y142 (≠ F141), E217 (= E209), D250 (= D242), N253 (≠ Q245), K280 (= K271), T309 (≠ G299), R408 (= R400)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ I53), Y84 (≠ I83), G115 (= G114), S116 (≠ A115), Y142 (≠ F141), H143 (= H142), D222 (≠ E214), D250 (= D242), V252 (= V244), N253 (≠ Q245), K280 (= K271), F308 (≠ G298), T309 (≠ G299), R408 (= R400)
Sites not aligning to the query:
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: 8:424/426 of query aligns to 33:459/474 of O58478
- D251 (≠ E214) mutation to A: Loss of activity.
- K308 (= K271) 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)
38% identity, 93% coverage: 31:426/426 of query aligns to 41:445/454 of O50131
- T92 (≠ Q82) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ I83) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G114) binding
- T125 (≠ A115) binding
- Q267 (= Q245) binding
- K293 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T300) binding
7vo1A Structure of aminotransferase-substrate complex (see paper)
38% identity, 93% coverage: 31:426/426 of query aligns to 39:443/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I53), S121 (≠ T113), G122 (= G114), T123 (≠ A115), F149 (= F141), H150 (= H142), R152 (= R144), E234 (= E214), D262 (= D242), V264 (= V244), Q265 (= Q245), K291 (= K271), N318 (≠ G299), T319 (= T300), R417 (= R400)
7vntA Structure of aminotransferase-substrate complex (see paper)
38% identity, 93% coverage: 31:426/426 of query aligns to 39:443/452 of 7vntA
- binding L-ornithine: F149 (= F141), R152 (= R144), E234 (= E214), K291 (= K271)
- binding pyridoxal-5'-phosphate: G122 (= G114), T123 (≠ A115), F149 (= F141), H150 (= H142), E229 (= E209), D262 (= D242), V264 (= V244), Q265 (= Q245), K291 (= K271)
7vnoA Structure of aminotransferase (see paper)
38% identity, 93% coverage: 31:426/426 of query aligns to 39:443/452 of 7vnoA
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)
34% identity, 93% coverage: 27:423/426 of query aligns to 25:400/405 of P40732
- GT 108:109 (≠ GA 114:115) binding
- K255 (= K271) modified: N6-(pyridoxal phosphate)lysine
- T284 (= T300) binding
4jevB N-acetylornithine aminotransferase from s. Typhimurium complexed with gabaculine
34% identity, 93% coverage: 27:423/426 of query aligns to 20:395/402 of 4jevB
- active site: F136 (= F141), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T279 (= T300), R372 (= R400)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: I46 (= I53), S102 (≠ T113), G103 (= G114), T104 (≠ A115), F136 (= F141), H137 (= H142), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), Q224 (= Q245), K250 (= K271), R372 (= R400)
4jewA N-acetylornithine aminotransferase from s. Typhimurium complexed with l-canaline
34% identity, 93% coverage: 27:423/426 of query aligns to 20:390/397 of 4jewA
- active site: F136 (= F141), E188 (= E209), D221 (= D242), Q224 (= Q245), K250 (= K271), T274 (= T300), R367 (= R400)
- binding (2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid: G103 (= G114), T104 (≠ A115), F136 (= F141), H137 (= H142), R139 (= R144), E188 (= E209), E193 (= E214), D221 (= D242), V223 (= V244), K250 (= K271)
- binding picric acid: K25 (≠ R32), K27 (≠ A34), W32 (= W39)
2pb0A Structure of biosynthetic n-acetylornithine aminotransferase from salmonella typhimurium: studies on substrate specificity and inhibitor binding (see paper)
34% identity, 93% coverage: 27:423/426 of query aligns to 14:384/389 of 2pb0A
- active site: F130 (= F141), E182 (= E209), D215 (= D242), Q218 (= Q245), K244 (= K271), T268 (= T300), R361 (= R400)
- binding pyridoxal-5'-phosphate: S96 (≠ T113), G97 (= G114), T98 (≠ A115), F130 (= F141), H131 (= H142), E182 (= E209), D215 (= D242), V217 (= V244), Q218 (= Q245), K244 (= K271)
Query Sequence
>HSERO_RS05420 HSERO_RS05420 4-aminobutyrate aminotransferase
MTSKANNQELQQRKNAATPRGVGVMCDFYAERAANAELWDVEGRRFIDFAAGIAVLNTGH
RHPKLLDAMRAQMDKFTHTAYQIVPYASYVELAERINRLTPGNYPKKTAFFSTGAEAVEN
AIKIARAHTGRPGVIAFAGGFHGRTMMGMALTGKVAPYKLGFGPFPGDVFHAPYPSALHG
ITSEDALEAVKGLFKSDIEAKRVAAIILEPVQGEGGFYAAPADFMRGLRALCDEHGILLI
ADEVQSGYGRTGKLFAMEHYDVLPDLMTMAKSLAGGMPLSAVNGRAEIMDAPAPGGLGGT
YAGNPLAIASALAVLDVMEEEQLVTRGQRLGDKLQEHLKELRSSVPQIAEVRGVGAMVAV
EFADPATGKPDAEYTKKVQQHALNNGLLLLTCGSYGNVIRFLFPLTIPDTVMDEALGILA
KAIRLA
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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