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Database: UniProt
Entry: A0A0C1G617_9RHOB
LinkDB: A0A0C1G617_9RHOB
Original site: A0A0C1G617_9RHOB 
ID   A0A0C1G617_9RHOB        Unreviewed;       253 AA.
AC   A0A0C1G617;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=RA27_20960 {ECO:0000313|EMBL:KIC37626.1};
OS   Ruegeria sp. ANG-R.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1577903 {ECO:0000313|EMBL:KIC37626.1, ECO:0000313|Proteomes:UP000031318};
RN   [1] {ECO:0000313|Proteomes:UP000031318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-R {ECO:0000313|Proteomes:UP000031318};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
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:KIC37626.1}.
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DR   EMBL; JWLJ01000013; KIC37626.1; -; Genomic_DNA.
DR   RefSeq; WP_039543574.1; NZ_JWLJ01000013.1.
DR   AlphaFoldDB; A0A0C1G617; -.
DR   STRING; 1577903.RA27_20960; -.
DR   OrthoDB; 9773478at2; -.
DR   Proteomes; UP000031318; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031318}.
SQ   SEQUENCE   253 AA;  27125 MW;  DFC688F26E4B5BC7 CRC64;
     MPHVDLNADM GESFGPWNMG DDDALLKIIT SANIACGFHA GDPDVMARTM ALAAENGVGI
     GAHPGFPDLQ GFGRRNMKVP HASLRNLVRY QLGAAIGMAK AVGTKVRHLK LHGALANMCS
     VDIDMARACY QGALDVDPDI IIMVLAVTRQ EDAVRELGCK WVGEIFADRA YNDDGTLVDR
     SFPGAVIHDP ELAGPRILSM VREGAIITES GKRLETSIDT ICLHGDGPTA VQIARSVRQN
     LIDGGVKVTK FIR
//
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