ID PUUE_ECOLI Reviewed; 421 AA.
AC P50457; P78150;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=4-aminobutyrate aminotransferase PuuE;
DE EC=2.6.1.19 {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:20639325};
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;
GN Name=puuE; Synonyms=goaG; OrderedLocusNames=b1302, JW1295;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Jovanovic G.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 FUNCTION AS A GABA AMINOTRANSFERASE, CATALYTIC ACTIVITY, PATHWAY, AND
RP NOMENCLATURE.
RC STRAIN=K12;
RX PubMed=15590624; DOI=10.1074/jbc.m411114200;
RA Kurihara S., Oda S., Kato K., Kim H.G., Koyanagi T., Kumagai H., Suzuki H.;
RT "A novel putrescine utilization pathway involves gamma-glutamylated
RT intermediates of Escherichia coli K-12.";
RL J. Biol. Chem. 280:4602-4608(2005).
RN [6]
RP FUNCTION IN PUTRESCINE DEGRADATION AND AS A GABA AMINOTRANSFERASE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-267,
RP DISRUPTION PHENOTYPE, ACTIVITY REGULATION, AND INDUCTION.
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).
CC -!- FUNCTION: Catalyzes the transfer of the amino group from gamma-
CC aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic
CC semialdehyde (SSA). PuuE is important for utilization of putrescine as
CC the sole nitrogen or carbon source. {ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:20639325}.
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:20639325};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353;
CC Evidence={ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:20639325};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Completely inhibited by succinate and low-aeration
CC conditions. {ECO:0000269|PubMed:20639325}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0577 mM for SSA (at pH 7.8 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:20639325};
CC KM=1.57 mM for GABA (at pH 7.8 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:20639325};
CC KM=5.1 mM for KG (at pH 7.8 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:20639325};
CC KM=18 mM for L-glutamate (at pH 7.8 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:20639325};
CC pH dependence:
CC Optimum pH is 9 for the forward reaction which is the transfer
CC reaction of the amino group from GABA to beta-ketoglutarate, and pH 8
CC for the reverse reaction. {ECO:0000269|PubMed:20639325};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation;
CC succinate semialdehyde from 4-aminobutanoate.
CC {ECO:0000269|PubMed:15590624}.
CC -!- INDUCTION: By putrescine. {ECO:0000269|PubMed:20639325}.
CC -!- DISRUPTION PHENOTYPE: Cells show only 35% of the wild-type activity.
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; U38543; AAC45301.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74384.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14871.1; -; Genomic_DNA.
DR PIR; A64879; A64879.
DR RefSeq; NP_415818.1; NC_000913.3.
DR RefSeq; WP_000069229.1; NZ_SSUW01000011.1.
DR PDB; 7JH3; X-ray; 2.68 A; A/B/C/D/E/F=1-421.
DR PDBsum; 7JH3; -.
DR AlphaFoldDB; P50457; -.
DR SMR; P50457; -.
DR BioGRID; 4263526; 17.
DR BioGRID; 849820; 1.
DR DIP; DIP-9825N; -.
DR IntAct; P50457; 3.
DR STRING; 511145.b1302; -.
DR PaxDb; 511145-b1302; -.
DR EnsemblBacteria; AAC74384; AAC74384; b1302.
DR GeneID; 945446; -.
DR KEGG; ecj:JW1295; -.
DR KEGG; eco:b1302; -.
DR PATRIC; fig|511145.12.peg.1358; -.
DR EchoBASE; EB2979; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR InParanoid; P50457; -.
DR OMA; GQMSCLL; -.
DR OrthoDB; 9801052at2; -.
DR PhylomeDB; P50457; -.
DR BioCyc; EcoCyc:G6646-MONOMER; -.
DR BioCyc; MetaCyc:G6646-MONOMER; -.
DR SABIO-RK; P50457; -.
DR PRO; PR:P50457; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IDA:EcoCyc.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..421
FT /note="4-aminobutyrate aminotransferase PuuE"
FT /id="PRO_0000120388"
FT BINDING 110..111
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 238..241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 267
FT /note="K->A: No GABA-AT activity."
FT /evidence="ECO:0000269|PubMed:20639325"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:7JH3"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:7JH3"
FT TURN 152..157
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:7JH3"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:7JH3"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:7JH3"
FT TURN 240..247
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 301..316
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 319..337
FT /evidence="ECO:0007829|PDB:7JH3"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:7JH3"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:7JH3"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:7JH3"
FT HELIX 405..420
FT /evidence="ECO:0007829|PDB:7JH3"
SQ SEQUENCE 421 AA; 44729 MW; A2C17A885FEBE4EB CRC64;
MSNNEFHQRR LSATPRGVGV MCNFFAQSAE NATLKDVEGN EYIDFAAGIA VLNTGHRHPD
LVAAVEQQLQ QFTHTAYQIV PYESYVTLAE KINALAPVSG QAKTAFFTTG AEAVENAVKI
ARAHTGRPGV IAFSGGFHGR TYMTMALTGK VAPYKIGFGP FPGSVYHVPY PSDLHGISTQ
DSLDAIERLF KSDIEAKQVA AIIFEPVQGE GGFNVAPKEL VAAIRRLCDE HGIVMIADEV
QSGFARTGKL FAMDHYADKP DLMTMAKSLA GGMPLSGVVG NANIMDAPAP GGLGGTYAGN
PLAVAAAHAV LNIIDKESLC ERANQLGQRL KNTLIDAKES VPAIAAVRGL GSMIAVEFND
PQTGEPSAAI AQKIQQRALA QGLLLLTCGA YGNVIRFLYP LTIPDAQFDA AMKILQDALS
D
//
