ID   PXPA_NEIMA              Reviewed;         245 AA.
AC   P0A0Z1; A1INQ0; Q9JQN2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE            Short=5-OPase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE            EC=3.5.2.9 {ECO:0000255|HAMAP-Rule:MF_00691};
DE   AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
GN   Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691}; Synonyms=rni3;
GN   OrderedLocusNames=NMA0030;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10722605; DOI=10.1128/iai.68.4.2082-2095.2000;
RA   Klee S.R., Nassif X., Kusecek B., Merker P., Beretti J.-L., Achtman M.,
RA   Tinsley C.R.;
RT   "Molecular and biological analysis of eight genetic islands that
RT   distinguish Neisseria meningitidis from the closely related pathogen
RT   Neisseria gonorrhoeae.";
RL   Infect. Immun. 68:2082-2095(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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}.
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   -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC       {ECO:0000255|HAMAP-Rule:MF_00691}.
CC   -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00691}.
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DR   EMBL; AJ391262; CAB72038.1; -; Genomic_DNA.
DR   EMBL; AL157959; CAM07357.1; -; Genomic_DNA.
DR   PIR; F81223; F81223.
DR   RefSeq; WP_002215593.1; NC_003116.1.
DR   AlphaFoldDB; P0A0Z1; -.
DR   SMR; P0A0Z1; -.
DR   EnsemblBacteria; CAM07357; CAM07357; NMA0030.
DR   KEGG; nma:NMA0030; -.
DR   HOGENOM; CLU_069535_0_0_4; -.
DR   OMA; DRTYKQD; -.
DR   BioCyc; NMEN122587:NMA_RS00150-MON; -.
DR   Proteomes; UP000000626; 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   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   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..245
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185019"
SQ   SEQUENCE   245 AA;  25983 MW;  F3A5BB07B77DB5D6 CRC64;
     MKQVDLNADL AEGCGSDEAL LQLITSANIA CAQHAGSIAD IRAALAYAQQ NGVRIGAHPG
     YPDRENFGRT EMNLSEADLR ACLNYQLGAL QALCRDQGLE MAYVKPHGAM YNQAAKNRAL
     ADTVARIVAD FDPKLKLMAL SGSLLLEAGK AAGLGVISEV FADRRYMPDG TLVPRSRPDA
     QVDSDEEAIA QVLQMVRDGQ VKAVDGSLVA VQADSICLHG DGPHAVVFAE KIRQELLAAG
     IKVSA