ID PXPB_HAEIN Reviewed; 213 AA.
AC P44299;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=5-oxoprolinase subunit B {ECO:0000250|UniProtKB:P0AAV4};
DE Short=5-OPase subunit B {ECO:0000250|UniProtKB:P0AAV4};
DE EC=3.5.2.9 {ECO:0000250|UniProtKB:P0AAV4};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit B {ECO:0000250|UniProtKB:P0AAV4};
GN Name=pxpB {ECO:0000250|UniProtKB:P0AAV4}; OrderedLocusNames=HI_1731;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:0000250|UniProtKB:P0AAV4}.
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:0000250|UniProtKB:P0AAV4};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000250|UniProtKB:P60495}.
CC -!- SIMILARITY: Belongs to the PxpB family. {ECO:0000305}.
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DR EMBL; L42023; AAC23377.1; -; Genomic_DNA.
DR PIR; C64041; C64041.
DR RefSeq; NP_439872.1; NC_000907.1.
DR AlphaFoldDB; P44299; -.
DR SMR; P44299; -.
DR STRING; 71421.HI_1731; -.
DR EnsemblBacteria; AAC23377; AAC23377; HI_1731.
DR KEGG; hin:HI_1731; -.
DR PATRIC; fig|71421.8.peg.1810; -.
DR eggNOG; COG2049; Bacteria.
DR HOGENOM; CLU_020207_0_0_6; -.
DR OrthoDB; 9778567at2; -.
DR PhylomeDB; P44299; -.
DR BioCyc; HINF71421:G1GJ1-1746-MONOMER; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR010016; PxpB.
DR NCBIfam; TIGR00370; 5-oxoprolinase subunit PxpB; 1.
DR PANTHER; PTHR34698; 5-OXOPROLINASE SUBUNIT B; 1.
DR PANTHER; PTHR34698:SF2; 5-OXOPROLINASE SUBUNIT B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..213
FT /note="5-oxoprolinase subunit B"
FT /id="PRO_0000168708"
SQ SEQUENCE 213 AA; 23641 MW; 1A2360FC83F2D77E CRC64;
MNIVPISESA VVCSLPPPAS IQQQRQLWAF ARQLQSEQDI VEVVLGMNNL TVFTDFFVDF
KPLVQRLEQL WAELKVSDFQ GRHIEIPVIY GGERGQDLSD VAKFHQTTPE RIIQMHSEPI
YTVYMIGFQA GFPYLGGLPE NLHTPRRATP RTVVPAGSVG IGGAQTGIYP FSSPGGWQLI
GYTKQALFDK NQAQPTLLQA GDTVKFIVEG IEL
//
