ID A0A1F8SF65_9CHLR Unreviewed; 259 AA.
AC A0A1F8SF65;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE RecName: Full=5-oxoprolinase subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
DE EC=3.5.2.9 {ECO:0000256|HAMAP-Rule:MF_00691};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
GN Name=pxpA {ECO:0000256|HAMAP-Rule:MF_00691};
GN ORFNames=A2V85_05845 {ECO:0000313|EMBL:OGO58527.1};
OS Chloroflexi bacterium RBG_16_72_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797663 {ECO:0000313|EMBL:OGO58527.1, ECO:0000313|Proteomes:UP000176218};
RN [1] {ECO:0000313|EMBL:OGO58527.1, ECO:0000313|Proteomes:UP000176218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:0000256|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:0000256|HAMAP-Rule:MF_00691};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000256|HAMAP-Rule:MF_00691}.
CC -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00691}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGO58527.1}.
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DR EMBL; MGOE01000038; OGO58527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SF65; -.
DR STRING; 1797663.A2V85_05845; -.
DR Proteomes; UP000176218; Unassembled WGS sequence.
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 CDD; cd10787; LamB_YcsF_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
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:SF0; 5-OXOPROLINASE SUBUNIT A; 1.
DR PANTHER; PTHR30292; UNCHARACTERIZED PROTEIN YBGL-RELATED; 1.
DR Pfam; PF03746; LamB_YcsF; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00691};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00691};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00691}.
SQ SEQUENCE 259 AA; 26436 MW; 7DB501B9A38C8397 CRC64;
MAGDATIDLN ADVGESFGAW PMGRDEALIP LVTSANVACG FHAGDPLVIR RTIALALASG
VAVGAHPGYP DLGGFGRRRL DMVADELSAA VEYQVAALAG MTRAAGGELR HVKPHGALYN
IAADDAAVAE AIVDGVARVS RDLVLVGMAG SALVAAGRAA GLAVSAEAFA DRAYEPNGRL
RSRRLPGAVH ADADAVVRQA LAIATGGPVI AFDGSRLRIE ADTLCLHGDT PGAVEHALAV
REAFAAHGIR VSADRELRG
//
