ID A0A451GCU3_9RHOB Unreviewed; 260 AA.
AC A0A451GCU3; A0A443JVE9; A0A443K917; A0A443KCT9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
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:RWR13254.1};
GN ORFNames=D2T29_15140 {ECO:0000313|EMBL:RWR29216.1}, D2T30_00750
GN {ECO:0000313|EMBL:RWR24471.1}, D2T31_06280
GN {ECO:0000313|EMBL:RWR30590.1}, D2T33_05930
GN {ECO:0000313|EMBL:RWR13254.1};
OS Sinirhodobacter populi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Sinirhodobacter.
OX NCBI_TaxID=2306993 {ECO:0000313|EMBL:RWR13254.1, ECO:0000313|Proteomes:UP000285710};
RN [1] {ECO:0000313|Proteomes:UP000284451, ECO:0000313|Proteomes:UP000284476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=07D10-4-3 {ECO:0000313|EMBL:RWR29216.1,
RC ECO:0000313|Proteomes:UP000284451}, 2D-5 {ECO:0000313|EMBL:RWR13254.1,
RC ECO:0000313|Proteomes:UP000285710}, D19-10-3-21
RC {ECO:0000313|EMBL:RWR30590.1, ECO:0000313|Proteomes:UP000285295}, and
RC SK2B-1 {ECO:0000313|EMBL:RWR24471.1,
RC ECO:0000313|Proteomes:UP000284476};
RA Xu G.;
RT "Sinorhodobacter populi sp. nov. isolated from the symptomatic bark tissue
RT of Populus euramericana canker.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000284451, ECO:0000313|Proteomes:UP000284476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=07D10-4-3 {ECO:0000313|EMBL:RWR29216.1,
RC ECO:0000313|Proteomes:UP000284451}, 2D-5 {ECO:0000313|EMBL:RWR13254.1,
RC ECO:0000313|Proteomes:UP000285710}, D19-10-3-21
RC {ECO:0000313|EMBL:RWR30590.1, ECO:0000313|Proteomes:UP000285295}, and
RC SK2B-1 {ECO:0000313|EMBL:RWR24471.1,
RC ECO:0000313|Proteomes:UP000284476};
RA Li Y.;
RL Submitted (JAN-2019) 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}.
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:RWR13254.1}.
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DR EMBL; SAUW01000005; RWR13254.1; -; Genomic_DNA.
DR EMBL; SAUZ01000001; RWR24471.1; -; Genomic_DNA.
DR EMBL; SAUY01000021; RWR29216.1; -; Genomic_DNA.
DR EMBL; SAUX01000007; RWR30590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A451GCU3; -.
DR OrthoDB; 5870696at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000284451; Unassembled WGS sequence.
DR Proteomes; UP000284476; Unassembled WGS sequence.
DR Proteomes; UP000285295; Unassembled WGS sequence.
DR Proteomes; UP000285710; 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:UP000285710}.
FT ACT_SITE 111
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 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 102..105
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ SEQUENCE 260 AA; 27926 MW; 78D1AC0F4BA6EBF5 CRC64;
MPADLSPIDK AKFAAAKCAS LLVEDGMKVG LGTGSTAAWM VRCLGERVRE EGLRITGVPT
STRTADLARQ LGIEIVSLDE AKWLDLTIDG ADEFDPELNL IKGGGGAHLL EKIVATASDR
MVVIADAAKE VAQLGAFPLP VEVVPFGWQT TRTIIEETLI SMDVLGRTTS LRQNGSQPFV
TDEGNYILDL HLNRIGNPRQ LAVTLNQIAG VVETGLFIDI CDMVVIGGAE GQVELRDIAA
GTVRQERIDF PDTVNIFTDL
//
