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4-aminobutyrate aminotransferase GabT (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (Glutamate:succinic semialdehyde transaminase) (L-AIBAT)

 GABT_ECOLI              Reviewed;         426 AA.
P22256;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
25-OCT-2017, entry version 158.
RecName: Full=4-aminobutyrate aminotransferase GabT;
EC=2.6.1.19;
AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
EC=2.6.1.22;
AltName: Full=GABA aminotransferase;
Short=GABA-AT;
AltName: Full=Gamma-amino-N-butyrate transaminase;
Short=GABA transaminase;
AltName: Full=Glutamate:succinic semialdehyde transaminase;
AltName: Full=L-AIBAT;
Name=gabT; OrderedLocusNames=b2662, JW2637;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2254272; DOI=10.1128/jb.172.12.7035-7042.1990;
Bartsch K., von Johnn-Marteville A., Schulz A.;
"Molecular analysis of two genes of the Escherichia coli gab cluster:
nucleotide sequence of the glutamate:succinic semialdehyde
transaminase gene (gabT) and characterization of the succinic
semialdehyde dehydrogenase gene (gabD).";
J. Bacteriol. 172:7035-7042(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-30.
STRAIN=K12;
PubMed=2178550;
Schulz A., Taggeselle P., Tripier D., Bartsch K.;
"Stereospecific production of the herbicide phosphinothricin
(glufosinate) by transamination: isolation and characterization of a
phosphinothricin-specific transaminase from Escherichia coli.";
Appl. Environ. Microbiol. 56:1-6(1990).
[6]
DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=12446648; DOI=10.1128/JB.184.24.6976-6986.2002;
Schneider B.L., Ruback S., Kiupakis A.K., Kasbarian H., Pybus C.,
Reitzer L.;
"The Escherichia coli gabDTPC operon: specific gamma-aminobutyrate
catabolism and nonspecific induction.";
J. Bacteriol. 184:6976-6986(2002).
[7]
INDUCTION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=14731280; DOI=10.1046/j.1365-2958.2003.03867.x;
Metzner M., Germer J., Hengge R.;
"Multiple stress signal integration in the regulation of the complex
sigma S-dependent csiD-ygaF-gabDTP operon in Escherichia coli.";
Mol. Microbiol. 51:799-811(2004).
[8]
FUNCTION AS A GABA AMINOTRANSFERASE, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=20639325; DOI=10.1128/JB.00308-10;
Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.;
"A putrescine-inducible pathway comprising PuuE-YneI in which gamma-
aminobutyrate is degraded into succinate in Escherichia coli K-12.";
J. Bacteriol. 192:4582-4591(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
5'-PHOSPHATE ANALOGS AND SUBUNIT.
STRAIN=K12;
PubMed=15323550; DOI=10.1021/bi049218e;
Liu W., Peterson P.E., Carter R.J., Zhou X., Langston J.A.,
Fisher A.J., Toney M.D.;
"Crystal structures of unbound and aminooxyacetate-bound Escherichia
coli gamma-aminobutyrate aminotransferase.";
Biochemistry 43:10896-10905(2004).
[10]
X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
5'-PHOSPHATE ANALOGS, COFACTOR, AND SUBUNIT.
STRAIN=K12;
PubMed=15723541; DOI=10.1021/bi048657a;
Liu W., Peterson P.E., Langston J.A., Jin X., Zhou X., Fisher A.J.,
Toney M.D.;
"Kinetic and crystallographic analysis of active site mutants of
Escherichia coli gamma-aminobutyrate aminotransferase.";
Biochemistry 44:2982-2992(2005).
-!- FUNCTION: Catalyzes the transfer of the amino group from gamma-
aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic
semialdehyde (SSA). {ECO:0000269|PubMed:20639325}.
-!- CATALYTIC ACTIVITY: 4-aminobutanoate + 2-oxoglutarate = succinate
semialdehyde + L-glutamate.
-!- CATALYTIC ACTIVITY: (S)-3-amino-2-methylpropanoate + 2-
oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:15723541};
-!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15323550,
ECO:0000269|PubMed:15723541}.
-!- INDUCTION: Induced by RpoS in response to multiple stress
conditions, including shifts to acidic pH or high osmolarity as
well as starvation or stationary phase. Catabolite repression by
glucose (repression relieved by GABA).
{ECO:0000269|PubMed:14731280}.
-!- DISRUPTION PHENOTYPE: Cells show only 68% of the wild-type
activity and are not able to utilize GABA as a nitrogen source.
{ECO:0000269|PubMed:12446648, ECO:0000269|PubMed:20639325}.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M88334; AAC36832.1; -; Genomic_DNA.
EMBL; U00096; AAC75709.1; -; Genomic_DNA.
EMBL; AP009048; BAA16525.1; -; Genomic_DNA.
PIR; A37846; A37846.
RefSeq; NP_417148.1; NC_000913.3.
RefSeq; WP_001087611.1; NZ_LN832404.1.
PDB; 1SF2; X-ray; 2.40 A; A/B/C/D=1-426.
PDB; 1SFF; X-ray; 1.90 A; A/B/C/D=1-426.
PDB; 1SZK; X-ray; 2.52 A; A/B/C/D=1-426.
PDB; 1SZS; X-ray; 2.10 A; A/B/C/D=1-426.
PDB; 1SZU; X-ray; 2.52 A; A/B/C/D=1-426.
PDBsum; 1SF2; -.
PDBsum; 1SFF; -.
PDBsum; 1SZK; -.
PDBsum; 1SZS; -.
PDBsum; 1SZU; -.
ProteinModelPortal; P22256; -.
SMR; P22256; -.
BioGrid; 4259210; 8.
DIP; DIP-9725N; -.
IntAct; P22256; 12.
MINT; MINT-1274800; -.
STRING; 316385.ECDH10B_2829; -.
DrugBank; DB02783; 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate.
DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
PaxDb; P22256; -.
PRIDE; P22256; -.
EnsemblBacteria; AAC75709; AAC75709; b2662.
EnsemblBacteria; BAA16525; BAA16525; BAA16525.
GeneID; 948067; -.
KEGG; ecj:JW2637; -.
KEGG; eco:b2662; -.
PATRIC; fig|1411691.4.peg.4079; -.
EchoBASE; EB0356; -.
EcoGene; EG10361; gabT.
eggNOG; ENOG4108JPW; Bacteria.
eggNOG; COG0160; LUCA.
HOGENOM; HOG000020206; -.
InParanoid; P22256; -.
KO; K07250; -.
PhylomeDB; P22256; -.
BioCyc; EcoCyc:GABATRANSAM-MONOMER; -.
BioCyc; MetaCyc:GABATRANSAM-MONOMER; -.
BRENDA; 2.6.1.19; 2026.
SABIO-RK; P22256; -.
UniPathway; UPA00733; -.
EvolutionaryTrace; P22256; -.
PRO; PR:P22256; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0003867; F:4-aminobutyrate transaminase activity; IDA:EcoCyc.
GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:EcoCyc.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
GO; GO:0042450; P:arginine biosynthetic process via ornithine; IGI:EcoCyc.
GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:EcoCyc.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004632; 4NH2But_aminotransferase_bac.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00700; GABAtrnsam; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
1: Evidence at protein level;
3D-structure; Aminotransferase; Complete proteome;
Direct protein sequencing; Pyridoxal phosphate; Reference proteome;
Transferase.
CHAIN 1 426 4-aminobutyrate aminotransferase GabT.
/FTId=PRO_0000120384.
REGION 111 112 Pyridoxal phosphate binding.
REGION 239 242 Pyridoxal phosphate binding.
BINDING 138 138 Pyridoxal phosphate.
BINDING 297 297 Pyridoxal phosphate.
MOD_RES 268 268 N6-(pyridoxal phosphate)lysine.
HELIX 4 14 {ECO:0000244|PDB:1SFF}.
STRAND 22 32 {ECO:0000244|PDB:1SFF}.
STRAND 34 37 {ECO:0000244|PDB:1SFF}.
STRAND 42 47 {ECO:0000244|PDB:1SFF}.
HELIX 48 51 {ECO:0000244|PDB:1SFF}.
HELIX 60 69 {ECO:0000244|PDB:1SFF}.
TURN 70 72 {ECO:0000244|PDB:1SFF}.
TURN 78 80 {ECO:0000244|PDB:1SFF}.
HELIX 84 96 {ECO:0000244|PDB:1SFF}.
STRAND 103 110 {ECO:0000244|PDB:1SFF}.
HELIX 111 126 {ECO:0000244|PDB:1SFF}.
STRAND 130 134 {ECO:0000244|PDB:1SFF}.
HELIX 143 148 {ECO:0000244|PDB:1SFF}.
TURN 153 158 {ECO:0000244|PDB:1SFF}.
STRAND 164 169 {ECO:0000244|PDB:1SFF}.
HELIX 174 176 {ECO:0000244|PDB:1SFF}.
HELIX 180 193 {ECO:0000244|PDB:1SFF}.
HELIX 197 199 {ECO:0000244|PDB:1SFF}.
STRAND 200 205 {ECO:0000244|PDB:1SFF}.
TURN 210 213 {ECO:0000244|PDB:1SFF}.
HELIX 219 232 {ECO:0000244|PDB:1SFF}.
STRAND 235 239 {ECO:0000244|PDB:1SFF}.
TURN 241 248 {ECO:0000244|PDB:1SFF}.
STRAND 249 252 {ECO:0000244|PDB:1SFF}.
HELIX 253 256 {ECO:0000244|PDB:1SFF}.
STRAND 262 266 {ECO:0000244|PDB:1SFF}.
HELIX 268 271 {ECO:0000244|PDB:1SFF}.
STRAND 273 275 {ECO:0000244|PDB:1SZK}.
STRAND 277 282 {ECO:0000244|PDB:1SFF}.
HELIX 283 286 {ECO:0000244|PDB:1SFF}.
STRAND 297 300 {ECO:0000244|PDB:1SFF}.
HELIX 302 317 {ECO:0000244|PDB:1SFF}.
HELIX 320 340 {ECO:0000244|PDB:1SFF}.
STRAND 345 351 {ECO:0000244|PDB:1SFF}.
STRAND 354 360 {ECO:0000244|PDB:1SFF}.
HELIX 361 363 {ECO:0000244|PDB:1SFF}.
HELIX 370 382 {ECO:0000244|PDB:1SFF}.
STRAND 388 391 {ECO:0000244|PDB:1SFF}.
STRAND 396 399 {ECO:0000244|PDB:1SFF}.
HELIX 407 424 {ECO:0000244|PDB:1SFF}.
SEQUENCE 426 AA; 45775 MW; 02FC80FF0EAA1361 CRC64;
MNSNKELMQR RSQAIPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI AVLNTGHLHP
KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD FAKKTLLVTT GSEAVENAVK
IARAATKRSG TIAFSGAYHG RTHYTLALTG KVNPYSAGMG LMPGHVYRAL YPCPLHGISE
DDAIASIHRI FKNDAAPEDI AAIVIEPVQG EGGFYASSPA FMQRLRALCD EHGIMLIADE
VQSGAGRTGT LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG
NPIACVAALE VLKVFEQENL LQKANDLGQK LKDGLLAIAE KHPEIGDVRG LGAMIAIELF
EDGDHNKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL VPLTIEDAQI RQGLEIISQC
FDEAKQ


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