PUUD_ECOLI
ID PUUD_ECOLI Reviewed; 254 AA.
AC P76038; P77761;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD;
DE Short=Gamma-Glu-GABA hydrolase;
DE EC=3.5.1.94;
GN Name=puuD; Synonyms=ycjL; OrderedLocusNames=b1298, JW1291;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 1-11, FUNCTION AS A GAMMA-GLUTAMYL-GAMMA-AMINOBUTYRATE
RP HYDROLASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INDUCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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 [5]
RP FUNCTION IN PUTRESCINE DEGRADATION AND AS A GAMMA-GLU-GABA HYDROLASE,
RP MUTAGENESIS OF CYS-114, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=16499623; DOI=10.1111/j.1574-6968.2006.00137.x;
RA Kurihara S., Oda S., Kumagai H., Suzuki H.;
RT "Gamma-glutamyl-gamma-aminobutyrate hydrolase in the putrescine utilization
RT pathway of Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 256:318-323(2006).
CC -!- FUNCTION: Involved in the breakdown of putrescine via hydrolysis of the
CC gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate.
CC {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:16499623}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(gamma-L-glutamylamino)butanoate + H2O = 4-aminobutanoate +
CC L-glutamate; Xref=Rhea:RHEA:19737, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58800, ChEBI:CHEBI:59888; EC=3.5.1.94;
CC Evidence={ECO:0000269|PubMed:15590624};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.93 mM for gamma-glutamyl-gamma-aminobutyrate
CC {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:16499623};
CC KM=18.5 mM for gamma-glutamylputrescine {ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:16499623};
CC pH dependence:
CC Optimum pH is between 8.5 and 9. {ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:16499623};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanoate from putrescine: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16499623}.
CC -!- INDUCTION: Induced by putrescine and nutrient starvation. Repressed by
CC PuuR and low aeration condition. Repressed at the exponential phase and
CC highly induced in early stationary phase. {ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:16499623}.
CC -!- DISRUPTION PHENOTYPE: Cells lose the hydrolase activity.
CC {ECO:0000269|PubMed:15590624}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR EMBL; U00096; AAC74380.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14858.1; -; Genomic_DNA.
DR PIR; E64878; E64878.
DR RefSeq; NP_415814.4; NC_000913.3.
DR RefSeq; WP_001300506.1; NZ_SSZK01000012.1.
DR PDB; 6VTV; X-ray; 2.06 A; A/B=1-254.
DR PDBsum; 6VTV; -.
DR AlphaFoldDB; P76038; -.
DR SMR; P76038; -.
DR BioGRID; 4260141; 29.
DR IntAct; P76038; 1.
DR STRING; 511145.b1298; -.
DR MEROPS; C26.961; -.
DR PaxDb; P76038; -.
DR PRIDE; P76038; -.
DR EnsemblBacteria; AAC74380; AAC74380; b1298.
DR EnsemblBacteria; BAA14858; BAA14858; BAA14858.
DR GeneID; 945882; -.
DR KEGG; ecj:JW1291; -.
DR KEGG; eco:b1298; -.
DR PATRIC; fig|511145.12.peg.1354; -.
DR EchoBASE; EB3668; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_0_0_6; -.
DR InParanoid; P76038; -.
DR OMA; PTYHHQA; -.
DR PhylomeDB; P76038; -.
DR BioCyc; EcoCyc:G6645-MON; -.
DR BioCyc; MetaCyc:G6645-MON; -.
DR BRENDA; 3.5.1.94; 2165.
DR UniPathway; UPA00188; UER00883.
DR PRO; PR:P76038; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0033969; F:gamma-glutamyl-gamma-aminobutyrate hydrolase activity; IDA:EcoCyc.
DR GO; GO:0006598; P:polyamine catabolic process; IBA:GO_Central.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR044668; PuuD-like.
DR PANTHER; PTHR43235; PTHR43235; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Reference proteome.
FT CHAIN 1..254
FT /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD"
FT /id="PRO_0000097110"
FT DOMAIN 16..250
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT MUTAGEN 114
FT /note="C->A: Lacks the PuuD activity. The expression level
FT is similar to that of the wild-type."
FT /evidence="ECO:0000269|PubMed:16499623"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6VTV"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:6VTV"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6VTV"
FT HELIX 231..253
FT /evidence="ECO:0007829|PDB:6VTV"
SQ SEQUENCE 254 AA; 28013 MW; ED183250300CCB42 CRC64;
MENIMNNPVI GVVMCRNRLK GHATQTLQEK YLNAIIHAGG LPIALPHALA EPSLLEQLLP
KLDGIYLPGS PSNVQPHLYG ENGDEPDADP GRDLLSMAII NAALERRIPI FAICRGLQEL
VVATGGSLHR KLCEQPELLE HREDPELPVE QQYAPSHEVQ VEEGGLLSAL LPECSNFWVN
SLHGQGAKVV SPRLRVEARS PDGLVEAVSV INHPFALGVQ WHPEWNSSEY ALSRILFEGF
ITACQHHIAE KQRL
