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