RPIA_METMP
ID RPIA_METMP Reviewed; 239 AA.
AC Q6LY04;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170};
GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; OrderedLocusNames=MMP1189;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR EMBL; BX950229; CAF30745.1; -; Genomic_DNA.
DR RefSeq; WP_011171133.1; NC_005791.1.
DR AlphaFoldDB; Q6LY04; -.
DR SMR; Q6LY04; -.
DR STRING; 267377.MMP1189; -.
DR PRIDE; Q6LY04; -.
DR EnsemblBacteria; CAF30745; CAF30745; MMP1189.
DR GeneID; 41279768; -.
DR KEGG; mmp:MMP1189; -.
DR PATRIC; fig|267377.15.peg.1222; -.
DR eggNOG; arCOG01122; Archaea.
DR HOGENOM; CLU_056590_1_1_2; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 98657at2157; -.
DR BioCyc; MMAR267377:MMP_RS06125-MON; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
DR CDD; cd01398; RPI_A; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR PANTHER; PTHR11934; PTHR11934; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome.
FT CHAIN 1..239
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158512"
FT ACT_SITE 119
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 40..43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 96..99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 110..113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ SEQUENCE 239 AA; 25658 MW; C1C40E851DF21457 CRC64;
MARTKKANDE VATDSDSLKL KVAKQAAKLV KDEMVVGLGS GSTANLFIQE LGKRVVEEEL
YIYGVPTSFD SRMMASNSGI PLISLDQCGE IDIAIDGADE VCKKTLSLIK GGGGCHTMEK
IVDYHAKEFV VLADEGKLVE SLGDKTAVPL EVIPFAYSTV LNKLLDMNTA PAIRSGSGKM
GPVITDNGNM IIDVFINIED AEETETMLNN IPGVLENGIF SKCDKVLVGT SKKVEILKK