PXPA_ECOLI
ID PXPA_ECOLI Reviewed; 244 AA.
AC P75746;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000305};
DE Short=5-OPase subunit A {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000305};
DE EC=3.5.2.9 {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000269|PubMed:28830929};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000305};
GN Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000303|PubMed:28830929};
GN Synonyms=ybgL; OrderedLocusNames=b0713, JW0703;
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=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(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 IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28830929; DOI=10.1074/jbc.m117.805028;
RA Niehaus T.D., Elbadawi-Sidhu M., de Crecy-Lagard V., Fiehn O., Hanson A.D.;
RT "Discovery of a widespread prokaryotic 5-oxoprolinase that was hiding in
RT plain sight.";
RL J. Biol. Chem. 292:16360-16367(2017).
RN [6] {ECO:0007744|PDB:1XW8}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA Kuzin A.P., Chen Y., Vorobiev S.M., Acton T.B., Ma L.-C., Xiao R.,
RA Montelione G.T., Hunt J.F., Tong L.;
RT "X-ray structure of putative lactam utilization protein YBGL. Northeast
RT Structural Genomics Consortium target ET90.";
RL Submitted (OCT-2004) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-glutamate
CC coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000269|PubMed:28830929}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00691,
CC ECO:0000269|PubMed:28830929};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000255|HAMAP-Rule:MF_00691}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene slows growth on minimal
CC medium with ammonium as nitrogen source. {ECO:0000269|PubMed:28830929}.
CC -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00691, ECO:0000305}.
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DR EMBL; U00096; AAC73807.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35377.1; -; Genomic_DNA.
DR PIR; H64806; H64806.
DR RefSeq; NP_415241.1; NC_000913.3.
DR RefSeq; WP_000687112.1; NZ_SSZK01000033.1.
DR PDB; 1XW8; X-ray; 2.00 A; A=1-244.
DR PDBsum; 1XW8; -.
DR AlphaFoldDB; P75746; -.
DR SMR; P75746; -.
DR BioGRID; 4259933; 106.
DR DIP; DIP-11398N; -.
DR IntAct; P75746; 4.
DR STRING; 511145.b0713; -.
DR jPOST; P75746; -.
DR PaxDb; P75746; -.
DR PRIDE; P75746; -.
DR EnsemblBacteria; AAC73807; AAC73807; b0713.
DR EnsemblBacteria; BAA35377; BAA35377; BAA35377.
DR GeneID; 945318; -.
DR KEGG; ecj:JW0703; -.
DR KEGG; eco:b0713; -.
DR PATRIC; fig|511145.12.peg.743; -.
DR EchoBASE; EB3092; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_6; -.
DR InParanoid; P75746; -.
DR OMA; DRTYKQD; -.
DR PhylomeDB; P75746; -.
DR BioCyc; EcoCyc:G6382-MON; -.
DR BioCyc; MetaCyc:G6382-MON; -.
DR EvolutionaryTrace; P75746; -.
DR PRO; PR:P75746; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR HAMAP; MF_00691; PxpA; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR005501; LamB/YcsF/PxpA-like.
DR PANTHER; PTHR30292; PTHR30292; 1.
DR Pfam; PF03746; LamB_YcsF; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..244
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_0000185007"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 75..95
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1XW8"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1XW8"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1XW8"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:1XW8"
SQ SEQUENCE 244 AA; 25800 MW; DBC0FD14ADA0EB0A CRC64;
MKIDLNADLG EGCASDAELL TLVSSANIAC GFHAGDAQIM QACVREAIKN GVAIGAHPSF
PDRENFGRSA MQLPPETVYA QTLYQIGALA TIARAQGGVM RHVKPHGMLY NQAAKEAQLA
DAIARAVYAC DPALILVGLA GSELIRAGKQ YGLTTREEVF ADRGYQADGS LVPRSQSGAL
IENEEQALAQ TLEMVQHGRV KSITGEWATV AAQTVCLHGD GEHALAFARR LRSAFAEKGI
VVAA
