PXPA3_PSEAE
ID PXPA3_PSEAE Reviewed; 251 AA.
AC Q9HVR0;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=5-oxoprolinase subunit A 3 {ECO:0000255|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_00691};
GN Name=pxpA3 {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=PA4511;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; AE004091; AAG07899.1; -; Genomic_DNA.
DR PIR; C83083; C83083.
DR RefSeq; NP_253201.1; NC_002516.2.
DR RefSeq; WP_003112852.1; NZ_QZGE01000004.1.
DR PDB; 2XU2; X-ray; 2.30 A; A=2-251.
DR PDBsum; 2XU2; -.
DR AlphaFoldDB; Q9HVR0; -.
DR SMR; Q9HVR0; -.
DR STRING; 287.DR97_1690; -.
DR PaxDb; Q9HVR0; -.
DR PRIDE; Q9HVR0; -.
DR DNASU; 881154; -.
DR EnsemblBacteria; AAG07899; AAG07899; PA4511.
DR GeneID; 881154; -.
DR KEGG; pae:PA4511; -.
DR PATRIC; fig|208964.12.peg.4721; -.
DR PseudoCAP; PA4511; -.
DR HOGENOM; CLU_069535_0_0_6; -.
DR InParanoid; Q9HVR0; -.
DR OMA; PHGELYF; -.
DR PhylomeDB; Q9HVR0; -.
DR BioCyc; PAER208964:G1FZ6-4600-MON; -.
DR BRENDA; 3.5.2.9; 5087.
DR EvolutionaryTrace; Q9HVR0; -.
DR Proteomes; UP000002438; 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..251
FT /note="5-oxoprolinase subunit A 3"
FT /id="PRO_0000185027"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2XU2"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 85..105
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2XU2"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2XU2"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:2XU2"
SQ SEQUENCE 251 AA; 27166 MW; E1AF77EEE2EB4655 CRC64;
MNDTGRRILL NCDMGESFGA WRMGDDVHSM PLVDQANLAC GFHAGDPLTM RRAVELAVRH
GVSIGAHPAY PDLSGFGRRS LACSAEEVHA MVLYQIGALD AFCRSLGTQV AYVKPHGALY
NDLVGDDELL RAVLDACAAY RKGLPLMVLA LADNGRELEL ADEADVPLLF EAFADRAYLP
DGRLAPRRLG GAVHHDPQRI IEQALAIARG EAFPDYDGNP LRLTADSLCV HGDNPQSLAV
LRRLRAALDS L
