PXPA_PYRHO
ID PXPA_PYRHO Reviewed; 255 AA.
AC O58714;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
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}; OrderedLocusNames=PH0986;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of lactam utilization protein from Pyrococcus horikoshii
RT OT3.";
RL Submitted (DEC-2004) to the PDB data bank.
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; BA000001; BAA30083.1; -; Genomic_DNA.
DR PIR; E71090; E71090.
DR RefSeq; WP_010885076.1; NC_000961.1.
DR PDB; 1V6T; X-ray; 1.70 A; A=1-255.
DR PDBsum; 1V6T; -.
DR AlphaFoldDB; O58714; -.
DR SMR; O58714; -.
DR MINT; O58714; -.
DR STRING; 70601.3257400; -.
DR EnsemblBacteria; BAA30083; BAA30083; BAA30083.
DR GeneID; 1443311; -.
DR KEGG; pho:PH0986; -.
DR eggNOG; arCOG05810; Archaea.
DR OMA; DRTYKQD; -.
DR OrthoDB; 47446at2157; -.
DR EvolutionaryTrace; O58714; -.
DR Proteomes; UP000000752; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Nucleotide-binding.
FT CHAIN 1..255
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_0000185066"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1V6T"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1V6T"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 80..100
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1V6T"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:1V6T"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1V6T"
SQ SEQUENCE 255 AA; 28431 MW; 1536EF00FDFA09B1 CRC64;
MRVDLNSDLG ESFGRYKLGL DEEVMKYITS ANVACGWHAG DPLVMRKTVR LAKENDVQVG
AHPGYPDLMG FGRRYMKLTP EEARNYILYQ VGALYAFAKA EGLELQHVKP HGALYNAMVK
EEDLARAVIE GILDFDKDLI LVTLSNSRVA DIAEEMGLKV AHEVFADRAY NPDGTLVPRG
RPGAVIEDKE EIAERVISMV KDGGIRAING EWVDLKVDTI CVHGDNPKAV EITSYIRKVL
EEEGVKIVPM KEFIR
