ID   PUUB_ECOLI              Reviewed;         426 AA.
AC   P37906; Q5H773;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Gamma-glutamylputrescine oxidoreductase;
DE            Short=Gamma-Glu-Put oxidase;
DE            Short=Gamma-glutamylputrescine oxidase;
DE            EC=1.4.3.-;
GN   Name=puuB; Synonyms=ordL, ycjA; OrderedLocusNames=b1301, JW1294;
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 [GENOMIC DNA], FUNCTION AS A GAMMA-GLUTAMYLPUTRESCINE
RP   OXIDOREDUCTASE, 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., 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   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
RX   PubMed=1840553; DOI=10.1016/0378-1119(91)90028-a;
RA   Heim R., Strehler E.E.;
RT   "Cloning an Escherichia coli gene encoding a protein remarkably similar to
RT   mammalian aldehyde dehydrogenases.";
RL   Gene 99:15-23(1991).
RN   [7]
RP   IDENTIFICATION.
RX   PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT   genome.";
RL   Nucleic Acids Res. 22:4756-4767(1994).
CC   -!- FUNCTION: Involved in the breakdown of putrescine via the oxidation of
CC       L-glutamylputrescine. {ECO:0000269|PubMed:15590624}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-L-glutamylputrescine + H2O + O2 = 4-(gamma-L-
CC         glutamylamino)butanal + H2O2 + NH4(+); Xref=Rhea:RHEA:28414,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58731, ChEBI:CHEBI:61508;
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC       aminobutanoate from putrescine: step 2/4.
CC   -!- SIMILARITY: Belongs to the gamma-glutamylputrescine oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; U38543; AAC45300.1; -; Genomic_DNA.
DR   EMBL; AB200320; BAD88709.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74383.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14870.1; -; Genomic_DNA.
DR   EMBL; M38433; AAA23429.1; -; Genomic_DNA.
DR   PIR; H64878; H64878.
DR   RefSeq; NP_415817.1; NC_000913.3.
DR   RefSeq; WP_000134870.1; NZ_SSZK01000012.1.
DR   AlphaFoldDB; P37906; -.
DR   SMR; P37906; -.
DR   BioGRID; 4263527; 12.
DR   IntAct; P37906; 18.
DR   STRING; 511145.b1301; -.
DR   PaxDb; P37906; -.
DR   PRIDE; P37906; -.
DR   EnsemblBacteria; AAC74383; AAC74383; b1301.
DR   EnsemblBacteria; BAA14870; BAA14870; BAA14870.
DR   GeneID; 945072; -.
DR   KEGG; ecj:JW1294; -.
DR   KEGG; eco:b1301; -.
DR   PATRIC; fig|1411691.4.peg.978; -.
DR   EchoBASE; EB1769; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_3_0_6; -.
DR   InParanoid; P37906; -.
DR   OMA; EQDAYLY; -.
DR   PhylomeDB; P37906; -.
DR   BioCyc; EcoCyc:EG11822-MON; -.
DR   BioCyc; MetaCyc:EG11822-MON; -.
DR   BRENDA; 1.4.3.B1; 2026.
DR   UniPathway; UPA00188; UER00881.
DR   PRO; PR:P37906; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IMP:UniProtKB.
DR   GO; GO:0009447; P:putrescine catabolic process; IMP:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..426
FT                   /note="Gamma-glutamylputrescine oxidoreductase"
FT                   /id="PRO_0000097109"
SQ   SEQUENCE   426 AA;  47170 MW;  44158FF418E9C254 CRC64;
     MTEHTSSYYA ASANKYAPFD TLNESITCDV CVVGGGYTGL SSALHLAEAG FDVVVLEASR
     IGFGASGRNG GQLVNSYSRD IDVIEKSYGM DTARMLGSMM FEGGEIIRER IKRYQIDCDY
     RPGGLFVAMN DKQLATLEEQ KENWERYGNK QLELLDANAI RREVASDRYT GALLDHSGGH
     IHPLNLAIGE ADAIRLNGGR VYELSAVTQI QHTTPAVVRT AKGQVTAKYV IVAGNAYLGD
     KVEPELAKRS MPCGTQVITT ERLSEDLARS LIPKNYCVED CNYLLDYYRL TADNRLLYGG
     GVVYGARDPD DVERLVVPKL LKTFPQLKGV KIDYRWTGNF LLTLSRMPQF GRLDTNIYYM
     QGYSGHGVTC THLAGRLIAE LLRGDAERFD AFANLPHYPF PGGRTLRVPF TAMGAAYYSL
     RDRLGV