GABT_ECOLI
ID GABT_ECOLI Reviewed; 426 AA.
AC P22256;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=4-aminobutyrate aminotransferase GabT;
DE EC=2.6.1.19 {ECO:0000269|PubMed:15723541, ECO:0000269|PubMed:30498244};
DE AltName: Full=5-aminovalerate transaminase {ECO:0000305|PubMed:30498244};
DE EC=2.6.1.48 {ECO:0000269|PubMed:30498244};
DE AltName: Full=GABA aminotransferase;
DE Short=GABA-AT;
DE AltName: Full=Gamma-amino-N-butyrate transaminase;
DE Short=GABA transaminase;
DE AltName: Full=Glutamate:succinic semialdehyde transaminase;
DE AltName: Full=L-AIBAT;
GN Name=gabT; OrderedLocusNames=b2662, JW2637;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2254272; DOI=10.1128/jb.172.12.7035-7042.1990;
RA Bartsch K., von Johnn-Marteville A., Schulz A.;
RT "Molecular analysis of two genes of the Escherichia coli gab cluster:
RT nucleotide sequence of the glutamate:succinic semialdehyde transaminase
RT gene (gabT) and characterization of the succinic semialdehyde dehydrogenase
RT gene (gabD).";
RL J. Bacteriol. 172:7035-7042(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-30.
RC STRAIN=K12;
RX PubMed=2178550; DOI=10.1128/aem.56.1.1-6.1990;
RA Schulz A., Taggeselle P., Tripier D., Bartsch K.;
RT "Stereospecific production of the herbicide phosphinothricin (glufosinate)
RT by transamination: isolation and characterization of a phosphinothricin-
RT specific transaminase from Escherichia coli.";
RL Appl. Environ. Microbiol. 56:1-6(1990).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=12446648; DOI=10.1128/jb.184.24.6976-6986.2002;
RA Schneider B.L., Ruback S., Kiupakis A.K., Kasbarian H., Pybus C.,
RA Reitzer L.;
RT "The Escherichia coli gabDTPC operon: specific gamma-aminobutyrate
RT catabolism and nonspecific induction.";
RL J. Bacteriol. 184:6976-6986(2002).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14731280; DOI=10.1046/j.1365-2958.2003.03867.x;
RA Metzner M., Germer J., Hengge R.;
RT "Multiple stress signal integration in the regulation of the complex sigma
RT S-dependent csiD-ygaF-gabDTP operon in Escherichia coli.";
RL Mol. Microbiol. 51:799-811(2004).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=20639325; DOI=10.1128/jb.00308-10;
RA Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.;
RT "A putrescine-inducible pathway comprising PuuE-YneI in which gamma-
RT aminobutyrate is degraded into succinate in Escherichia coli K-12.";
RL J. Bacteriol. 192:4582-4591(2010).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=K12 / BW25113;
RX PubMed=30498244; DOI=10.1038/s41467-018-07563-6;
RA Knorr S., Sinn M., Galetskiy D., Williams R.M., Wang C., Mueller N.,
RA Mayans O., Schleheck D., Hartig J.S.;
RT "Widespread bacterial lysine degradation proceeding via glutarate and L-2-
RT hydroxyglutarate.";
RL Nat. Commun. 9:5071-5071(2018).
RN [10] {ECO:0007744|PDB:1SF2, ECO:0007744|PDB:1SFF}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP 5'-PHOSPHATE OR THE AMINOOXYACETATE INHIBITOR, COFACTOR, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=15323550; DOI=10.1021/bi049218e;
RA Liu W., Peterson P.E., Carter R.J., Zhou X., Langston J.A., Fisher A.J.,
RA Toney M.D.;
RT "Crystal structures of unbound and aminooxyacetate-bound Escherichia coli
RT gamma-aminobutyrate aminotransferase.";
RL Biochemistry 43:10896-10905(2004).
RN [11] {ECO:0007744|PDB:1SZK, ECO:0007744|PDB:1SZS, ECO:0007744|PDB:1SZU}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS GLN-50; SER-211 AND
RP ALA-241 IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF
RP ILE-50; GLU-211 AND VAL-241, AND REACTION MECHANISM.
RC STRAIN=K12;
RX PubMed=15723541; DOI=10.1021/bi048657a;
RA Liu W., Peterson P.E., Langston J.A., Jin X., Zhou X., Fisher A.J.,
RA Toney M.D.;
RT "Kinetic and crystallographic analysis of active site mutants of
RT Escherichia coli gamma-aminobutyrate aminotransferase.";
RL Biochemistry 44:2982-2992(2005).
CC -!- FUNCTION: Pyridoxal phosphate-dependent enzyme that catalyzes
CC transamination between primary amines and alpha-keto acids. Catalyzes
CC the transfer of the amino group from gamma-aminobutyrate (GABA) to
CC alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and
CC glutamate (PubMed:15723541, PubMed:30498244). Thereby functions in a
CC GABA degradation pathway that allows some E.coli strains to utilize
CC GABA as a nitrogen source for growth (PubMed:12446648). Also catalyzes
CC the conversion of 5-aminovalerate to glutarate semialdehyde, as part of
CC a L-lysine degradation pathway that proceeds via cadaverine, glutarate
CC and L-2-hydroxyglutarate (PubMed:30498244).
CC {ECO:0000269|PubMed:12446648, ECO:0000269|PubMed:15723541,
CC ECO:0000269|PubMed:30498244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC Evidence={ECO:0000269|PubMed:15723541, ECO:0000269|PubMed:30498244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353;
CC Evidence={ECO:0000269|PubMed:12446648};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:10212, ChEBI:CHEBI:16120,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:356010;
CC EC=2.6.1.48; Evidence={ECO:0000269|PubMed:30498244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10213;
CC Evidence={ECO:0000305|PubMed:30498244};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15323550, ECO:0000269|PubMed:15723541};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=197 uM for 4-aminobutanoate (measured for a coupled GabT/GabD
CC reaction) {ECO:0000269|PubMed:30498244};
CC KM=439 uM for 5-aminopentanoate (measured for a coupled GabT/GabD
CC reaction) {ECO:0000269|PubMed:30498244};
CC KM=5.8 mM for 4-aminobutanoate (at 25 degrees Celsius and pH 7.8)
CC {ECO:0000269|PubMed:15723541};
CC KM=1.07 mM for 2-oxoglutarate (at 25 degrees Celsius and pH 7.8)
CC {ECO:0000269|PubMed:15723541};
CC Note=kcat is 47.4 sec(-1) with 4-aminobutanoate as substrate (at 25
CC degrees Celsius and pH 7.8). {ECO:0000269|PubMed:15723541};
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC {ECO:0000269|PubMed:12446648}.
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:30498244}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15323550,
CC ECO:0000269|PubMed:15723541}.
CC -!- INDUCTION: Induced by RpoS in response to multiple stress conditions,
CC including shifts to acidic pH or high osmolarity as well as starvation
CC or stationary phase. Catabolite repression by glucose (repression
CC relieved by GABA) (PubMed:14731280). Makes part of the gabDTPC operon,
CC which is up-regulated by nitrogen limitation (PubMed:12446648).
CC {ECO:0000269|PubMed:12446648, ECO:0000269|PubMed:14731280}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to utilize
CC GABA as a nitrogen source, in contrast to wild-type, but grow normally
CC with arginine, ornithine, putrescine and agmatine (PubMed:12446648).
CC Cells show only 68% of the wild-type GABA aminotransferase activity
CC (PubMed:20639325). {ECO:0000269|PubMed:12446648,
CC ECO:0000269|PubMed:20639325}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M88334; AAC36832.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75709.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16525.1; -; Genomic_DNA.
DR PIR; A37846; A37846.
DR RefSeq; NP_417148.1; NC_000913.3.
DR RefSeq; WP_001087611.1; NZ_LN832404.1.
DR PDB; 1SF2; X-ray; 2.40 A; A/B/C/D=1-426.
DR PDB; 1SFF; X-ray; 1.90 A; A/B/C/D=1-426.
DR PDB; 1SZK; X-ray; 2.52 A; A/B/C/D=1-426.
DR PDB; 1SZS; X-ray; 2.10 A; A/B/C/D=1-426.
DR PDB; 1SZU; X-ray; 2.52 A; A/B/C/D=1-426.
DR PDBsum; 1SF2; -.
DR PDBsum; 1SFF; -.
DR PDBsum; 1SZK; -.
DR PDBsum; 1SZS; -.
DR PDBsum; 1SZU; -.
DR AlphaFoldDB; P22256; -.
DR SMR; P22256; -.
DR BioGRID; 4259210; 22.
DR BioGRID; 852375; 2.
DR DIP; DIP-9725N; -.
DR IntAct; P22256; 12.
DR STRING; 511145.b2662; -.
DR DrugBank; DB02783; 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate.
DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR jPOST; P22256; -.
DR PaxDb; P22256; -.
DR PRIDE; P22256; -.
DR EnsemblBacteria; AAC75709; AAC75709; b2662.
DR EnsemblBacteria; BAA16525; BAA16525; BAA16525.
DR GeneID; 948067; -.
DR KEGG; ecj:JW2637; -.
DR KEGG; eco:b2662; -.
DR PATRIC; fig|1411691.4.peg.4079; -.
DR EchoBASE; EB0356; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR InParanoid; P22256; -.
DR OMA; TSGQMSC; -.
DR PhylomeDB; P22256; -.
DR BioCyc; EcoCyc:GABATRANSAM-MON; -.
DR BioCyc; MetaCyc:GABATRANSAM-MON; -.
DR BRENDA; 2.6.1.19; 2026.
DR SABIO-RK; P22256; -.
DR UniPathway; UPA00733; -.
DR EvolutionaryTrace; P22256; -.
DR PRO; PR:P22256; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IDA:EcoCyc.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IDA:EcoCyc.
DR GO; GO:0047589; F:5-aminovalerate transaminase activity; IDA:EcoCyc.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:EcoCyc.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Direct protein sequencing;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..426
FT /note="4-aminobutyrate aminotransferase GabT"
FT /id="PRO_0000120384"
FT BINDING 111..112
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:15323550,
FT ECO:0000269|PubMed:15723541"
FT BINDING 242
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:15323550,
FT ECO:0000269|PubMed:15723541"
FT BINDING 297
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:15323550,
FT ECO:0000269|PubMed:15723541"
FT MOD_RES 268
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:15323550,
FT ECO:0000269|PubMed:15723541, ECO:0007744|PDB:1SF2,
FT ECO:0007744|PDB:1SZS, ECO:0007744|PDB:1SZU"
FT MUTAGEN 50
FT /note="I->Q: 3-fold decrease in catalytic activity and 12-
FT fold decrease in affinity for GABA."
FT /evidence="ECO:0000269|PubMed:15723541"
FT MUTAGEN 211
FT /note="E->S: 100-fold decrease in catalytic activity and
FT 15-fold decrease in affinity for GABA."
FT /evidence="ECO:0000269|PubMed:15723541"
FT MUTAGEN 241
FT /note="V->A: 25-fold decrease in catalytic activity and 5-
FT fold decrease in affinity for GABA."
FT /evidence="ECO:0000269|PubMed:15723541"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 22..32
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:1SFF"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1SFF"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:1SFF"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:1SFF"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1SFF"
FT TURN 241..248
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1SZK"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 320..340
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:1SFF"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:1SFF"
FT HELIX 407..424
FT /evidence="ECO:0007829|PDB:1SFF"
SQ 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
