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Database: UniProt
Entry: H8MW96_CORCM
LinkDB: H8MW96_CORCM
Original site: H8MW96_CORCM 
ID   H8MW96_CORCM            Unreviewed;       235 AA.
AC   H8MW96;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE            EC=5.3.1.6 {ECO:0000256|HAMAP-Rule:MF_00170};
DE   AltName: Full=Phosphoriboisomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE            Short=PRI {ECO:0000256|HAMAP-Rule:MF_00170};
GN   Name=rpiA {ECO:0000256|HAMAP-Rule:MF_00170,
GN   ECO:0000313|EMBL:AFE10193.1};
GN   OrderedLocusNames=COCOR_06641 {ECO:0000313|EMBL:AFE10193.1};
OS   Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS   (Myxococcus coralloides).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Corallococcus.
OX   NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE10193.1, ECO:0000313|Proteomes:UP000007587};
RN   [1] {ECO:0000313|EMBL:AFE10193.1, ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RX   PubMed=22582372; DOI=10.1128/JB.00397-12;
RA   Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA   Sogaard-Andersen L.;
RT   "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT   coralloides DSM 2259.";
RL   J. Bacteriol. 194:3012-3013(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RA   Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT   "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT   DSM 2259.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC       ribulose 5-phosphate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00170}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00170}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00170}.
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DR   EMBL; CP003389; AFE10193.1; -; Genomic_DNA.
DR   RefSeq; WP_014399428.1; NC_017030.1.
DR   AlphaFoldDB; H8MW96; -.
DR   STRING; 1144275.COCOR_06641; -.
DR   KEGG; ccx:COCOR_06641; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_1_7; -.
DR   InParanoid; H8MW96; -.
DR   OrthoDB; 5870696at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000007587; 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   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.1360; -; 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   NCBIfam; TIGR00021; rpiA; 1.
DR   PANTHER; PTHR43748; RIBOSE-5-PHOSPHATE ISOMERASE 3, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43748:SF3; RIBOSE-5-PHOSPHATE ISOMERASE 3, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF75445; D-ribose-5-phosphate isomerase (RpiA), lid domain; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007587}.
FT   ACT_SITE        112
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         33..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         90..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         103..106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   235 AA;  24296 MW;  22E93BDEF0D8B540 CRC64;
     MTSDESVSAS LKRAAAERAV DFIQPGMVVG LGTGSTAAYA VRRLGALLSS GTLKDVVGIP
     TSHATETLAA SLGVPLTTLD VHPVVDLTID GADEVAPDLS LIKGGGGALL REKVVAQASR
     REIIVVDAVK LSPRLGTKWP VPVEVLPFGW RSQALFLESL GARVVVRLAL DGAPYHTDQG
     NVVLDCDFGP IGDPAALAAK LESRAGVMAH GLFLNLTTDL VVAGPEGITH RVRGA
//
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