ID W7QHZ3_9ALTE Unreviewed; 217 AA.
AC W7QHZ3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=DS2_03295 {ECO:0000313|EMBL:EWH11501.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH11501.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH11501.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH11501.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWH11501.1}.
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DR EMBL; ARZY01000004; EWH11501.1; -; Genomic_DNA.
DR RefSeq; WP_035013221.1; NZ_ARZY01000004.1.
DR AlphaFoldDB; W7QHZ3; -.
DR STRING; 1328313.DS2_03295; -.
DR PATRIC; fig|1328313.3.peg.684; -.
DR eggNOG; COG0120; Bacteria.
DR OrthoDB; 5870696at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000019276; Unassembled WGS sequence.
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; PTHR11934; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11934:SF0; RIBOSE-5-PHOSPHATE ISOMERASE; 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:UP000019276}.
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 28..31
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 94..97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ SEQUENCE 217 AA; 23094 MW; D7E643349010F599 CRC64;
MNQNDKKKAV AEAAIQYVEK GSIVGVGTGS TTNFFIDALA PIADDLKGAV SSSEASTERL
KALGIEVFDL NEVSSFDIYV DGADEVNPQS HMIKGGGAAL TREKIVAAVA KRFICIVDDS
KEVDVMGNFP LPVEVIPMAR SYVAREIVKL GGDPVYRQGV VTDNGNVILD VHNLQITDAI
ELETKLNQIT GVVTNGLFAM RGADVVLVAT DNGVKTR
//
