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Database: UniProt/SWISS-PROT
Entry: RPIA_METVS
LinkDB: RPIA_METVS
Original site: RPIA_METVS 
ID   RPIA_METVS              Reviewed;         239 AA.
AC   A6UPJ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   14-MAY-2014, entry version 40.
DE   RecName: Full=Ribose-5-phosphate isomerase A;
DE            EC=5.3.1.6;
DE   AltName: Full=Phosphoriboisomerase A;
DE            Short=PRI;
GN   Name=rpiA; OrderedLocusNames=Mevan_0505;
OS   Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB / ATCC 35089 / DSM 1224;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-
CC       phosphate to ribulose 5-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative
CC       stage): step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
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DR   EMBL; CP000742; ABR54412.1; -; Genomic_DNA.
DR   RefSeq; YP_001323024.1; NC_009634.1.
DR   ProteinModelPortal; A6UPJ0; -.
DR   SMR; A6UPJ0; 15-239.
DR   STRING; 406327.Mevan_0505; -.
DR   EnsemblBacteria; ABR54412; ABR54412; Mevan_0505.
DR   GeneID; 5325659; -.
DR   KEGG; mvn:Mevan_0505; -.
DR   eggNOG; COG0120; -.
DR   HOGENOM; HOG000276369; -.
DR   KO; K01807; -.
DR   OMA; MDQLEMK; -.
DR   BioCyc; MVAN406327:GI04-510-MONOMER; -.
DR   UniPathway; UPA00115; UER00412.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR   InterPro; IPR004788; Ribose5P_isomerase_typA.
DR   InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR   PANTHER; PTHR11934; PTHR11934; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   TIGRFAMs; TIGR00021; rpiA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase.
FT   CHAIN         1    239       Ribose-5-phosphate isomerase A.
FT                                /FTId=PRO_1000016950.
FT   REGION       40     43       Substrate binding (By similarity).
FT   REGION       96     99       Substrate binding (By similarity).
FT   REGION      110    113       Substrate binding (By similarity).
FT   ACT_SITE    119    119       Proton acceptor (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
SQ   SEQUENCE   239 AA;  25842 MW;  E410F8ACA7599C53 CRC64;
     MAKPKKSDEE VSIDSDSLKI KVAKEAAKLI KDEMVVGLGS GSTANLFIQE LGKRVIEEEL
     YIYGVPTSFD SRMMANQSGI PLISLDQCGE IDIAIDGADE IDKKTFSLIK GGGGCHTMEK
     IVDYYAKEFV VLADESKMVD SLGENTPVPL EVIPFSYSTV LSKLLKINAA PAIRSGSGKM
     GPVITDNGNM IIDVFINIED AEETETMLNS IPGVLENGIF TKCDKVLIGT SKKVEVLKK
//
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