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
//