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Database: UniProt
Entry: A0A433S6S2_9RHOB
LinkDB: A0A433S6S2_9RHOB
Original site: A0A433S6S2_9RHOB 
ID   A0A433S6S2_9RHOB        Unreviewed;       262 AA.
AC   A0A433S6S2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
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:RUS63268.1};
GN   ORFNames=EGN72_05250 {ECO:0000313|EMBL:RUS63268.1};
OS   Pseudorhodobacter sp. E13.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudorhodobacter.
OX   NCBI_TaxID=2487931 {ECO:0000313|EMBL:RUS63268.1, ECO:0000313|Proteomes:UP000267424};
RN   [1] {ECO:0000313|EMBL:RUS63268.1, ECO:0000313|Proteomes:UP000267424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E13 {ECO:0000313|EMBL:RUS63268.1,
RC   ECO:0000313|Proteomes:UP000267424};
RA   Lee H., Kim S.;
RT   "Pseudorhodobacter sp. isolated from seawater.";
RL   Submitted (NOV-2018) 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:RUS63268.1}.
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DR   EMBL; RPEN01000148; RUS63268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433S6S2; -.
DR   OrthoDB; 5870696at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000267424; 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; 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:UP000267424}.
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   262 AA;  28233 MW;  DF712519D5D6E3B0 CRC64;
     MAAELSPIDK AKFVAAKRAV EFVENGMKLG LGTGSTAAWM VRCLAERIRE DGLRVTGVPT
     SSRTAELARS LGVPITSLDE ARWLDLTIDG ADEFDPSLNL IKGGGAALLQ EKIVATASDQ
     MIVITDAAKE VAQLGAFPLP VEVIPFGWQT TKALLEEMLV SMDVLNRECS LRMNGAAPLV
     TDEGNYIVDM HLRRIGNARQ LAMVLNQIPG VVENGLFIDI CDIVVIGHGD GRVVVRDINS
     GEVEDDRVEF VPSDNIFADM GD
//
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