RPIA_METM6
ID RPIA_METM6 Reviewed; 239 AA.
AC A9AAC4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=MmarC6_1484;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX02297.1; -; Genomic_DNA.
DR RefSeq; WP_012194217.1; NC_009975.1.
DR AlphaFoldDB; A9AAC4; -.
DR SMR; A9AAC4; -.
DR STRING; 444158.MmarC6_1484; -.
DR EnsemblBacteria; ABX02297; ABX02297; MmarC6_1484.
DR GeneID; 5737649; -.
DR KEGG; mmx:MmarC6_1484; -.
DR eggNOG; arCOG01122; Archaea.
DR HOGENOM; CLU_056590_1_1_2; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 98657at2157; -.
DR PhylomeDB; A9AAC4; -.
DR UniPathway; UPA00115; UER00412.
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.
FT CHAIN 1..239
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_1000097675"
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; 25648 MW; 7D93E16331B956EE CRC64;
MARTKKANDE VPTDSDSLKL KVAKQAAKLV KDEMVVGLGS GSTANLFIQE LGKRIVEEEL
YIYGVPTSFD SRMVASTAGI PLISLDQCGE IDIAVDGADE VCKSTLSLIK GGGGCHTMEK
IVDYHAKEFI VLADEGKLVD SLGDKTPVPL EVIPFAYSTI LNKLLKMNTA PVIRTGSGKM
GPVITDNGNM IIDVFISIDD AEETEIMLNN IPGVLENGVF SKCDKVLIGT SKKVEILKK
