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Database: UniProt/SWISS-PROT
Entry: PUUE_ECOLI
LinkDB: PUUE_ECOLI
Original site: PUUE_ECOLI 
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   28-MAR-2018, entry version 137.
DE   RecName: Full=4-aminobutyrate aminotransferase PuuE;
DE            EC=2.6.1.19;
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; Proteobacteria; 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.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION AS A GABA AMINOTRANSFERASE, AND 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.,
RA   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   BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-267, DISRUPTION
RP   PHENOTYPE, ENZYME 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
CC       putrescine as the sole nitrogen or carbon source.
CC       {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:20639325}.
CC   -!- CATALYTIC ACTIVITY: 4-aminobutanoate + 2-oxoglutarate = succinate
CC       semialdehyde + L-glutamate.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- ENZYME REGULATION: Completely inhibited by succinate and low-
CC       aeration 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
CC         pH 8 for the reverse reaction. {ECO:0000269|PubMed:20639325};
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation;
CC       succinate semialdehyde from 4-aminobutanoate: step 1/1.
CC   -!- INDUCTION: By putrescine. {ECO:0000269|PubMed:20639325}.
CC   -!- DISRUPTION PHENOTYPE: Cells show only 35% of the wild-type
CC       activity. {ECO:0000269|PubMed:20639325}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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_LN832404.1.
DR   ProteinModelPortal; P50457; -.
DR   SMR; P50457; -.
DR   BioGrid; 4263526; 17.
DR   DIP; DIP-9825N; -.
DR   IntAct; P50457; 3.
DR   STRING; 316385.ECDH10B_1419; -.
DR   PaxDb; P50457; -.
DR   PRIDE; P50457; -.
DR   EnsemblBacteria; AAC74384; AAC74384; b1302.
DR   EnsemblBacteria; BAA14871; BAA14871; BAA14871.
DR   GeneID; 945446; -.
DR   KEGG; ecj:JW1295; -.
DR   KEGG; eco:b1302; -.
DR   PATRIC; fig|511145.12.peg.1358; -.
DR   EchoBASE; EB2979; -.
DR   EcoGene; EG13187; puuE.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   InParanoid; P50457; -.
DR   KO; K00823; -.
DR   OMA; GMTTQIY; -.
DR   PhylomeDB; P50457; -.
DR   BioCyc; EcoCyc:G6646-MONOMER; -.
DR   BioCyc; MetaCyc:G6646-MONOMER; -.
DR   SABIO-RK; P50457; -.
DR   UniPathway; UPA00188; UER00293.
DR   PRO; PR:P50457; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
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:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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   Aminotransferase; Complete proteome; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN         1    421       4-aminobutyrate aminotransferase PuuE.
FT                                /FTId=PRO_0000120388.
FT   REGION      110    111       Pyridoxal phosphate binding.
FT                                {ECO:0000250}.
FT   REGION      238    241       Pyridoxal phosphate binding.
FT                                {ECO:0000250}.
FT   BINDING     296    296       Pyridoxal phosphate. {ECO:0000250}.
FT   MOD_RES     267    267       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   MUTAGEN     267    267       K->A: No GABA-AT activity.
FT                                {ECO:0000269|PubMed:20639325}.
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
//
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