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RPIA2_OCEIH
ID   RPIA2_OCEIH             Reviewed;         224 AA.
AC   Q8EMZ1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Ribose-5-phosphate isomerase A 2 {ECO:0000255|HAMAP-Rule:MF_00170};
DE            EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE   AltName: Full=Phosphoriboisomerase A 2 {ECO:0000255|HAMAP-Rule:MF_00170};
DE            Short=PRI 2 {ECO:0000255|HAMAP-Rule:MF_00170};
GN   Name=rpiA2 {ECO:0000255|HAMAP-Rule:MF_00170}; OrderedLocusNames=OB2699;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC14655.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8EMZ1; -.
DR   SMR; Q8EMZ1; -.
DR   STRING; 221109.22778386; -.
DR   EnsemblBacteria; BAC14655; BAC14655; BAC14655.
DR   KEGG; oih:OB2699; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_0_9; -.
DR   PhylomeDB; Q8EMZ1; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000000822; 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   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..224
FT                   /note="Ribose-5-phosphate isomerase A 2"
FT                   /id="PRO_0000158442"
FT   ACT_SITE        105
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         27..30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         83..86
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         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   224 AA;  24828 MW;  4AF307FEC363E154 CRC64;
     MEYSDKQIAA QEAVRYIKDG MVIGIGSGST VNEFLYCLAA RMRKERLQVV GIPASKKSER
     LATELGIPLT TFATYQNVDI AIDGTDEIDD QLYLVKGGGG SLVREKMIDL VAETFIVIAS
     GKKKIKKLGS FPVPVEVVPF GWQATEQRLQ QFGCQTNLRM VEEDIFVSDN QNYIIDCDFK
     EIDDAEALHR SLKQIVGVIE TGIFINMVDK AIVADNGELS ILEK
 
 
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