(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NQQ6_YERPA

ID   A0A0E1NQQ6_YERPA        Unreviewed;       218 AA.
AC   A0A0E1NQQ6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 25.
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   OrderedLocusNames=YPA_0352 {ECO:0000313|EMBL:ABG12320.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12320.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12320.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12320.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-
CC       phosphate to ribulose 5-phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00170, ECO:0000256|SAAS:SAAS00731113}.
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         ECO:0000256|SAAS:SAAS01124525};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative
CC       stage): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00170,
CC       ECO:0000256|SAAS:SAAS00731128}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00170,
CC       ECO:0000256|SAAS:SAAS00731108}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00170, ECO:0000256|SAAS:SAAS00731110}.
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DR   EMBL; CP000308; ABG12320.1; -; Genomic_DNA.
DR   RefSeq; WP_002209957.1; NZ_CP009906.1.
DR   SMR; A0A0E1NQQ6; -.
DR   EnsemblBacteria; ABG12320; ABG12320; YPA_0352.
DR   EnsemblBacteria; AJJ79220; AJJ79220; CH58_3200.
DR   KEGG; ypa:YPA_0352; -.
DR   PATRIC; fig|360102.15.peg.3359; -.
DR   KO; K01807; -.
DR   OMA; VAPMAYV; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001971; 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; IPR004788; Ribose5P_isomerase_typA.
DR   InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR   PANTHER; PTHR11934; PTHR11934; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00021; rpiA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NQQ6.
DR   SWISS-2DPAGE; A0A0E1NQQ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00170,
KW   ECO:0000256|SAAS:SAAS01090754, ECO:0000313|EMBL:ABG12320.1}.
FT   REGION       28     31       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00170}.
FT   REGION       81     84       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00170}.
FT   REGION       94     97       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00170}.
FT   ACT_SITE    103    103       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00170}.
FT   BINDING     121    121       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00170}.
SQ   SEQUENCE   218 AA;  22801 MW;  44902D266E9EBE1C CRC64;
     MTQDELKKAV GWAALDYVKP GTIVGVGTGS TAAHFIDALG SIKHQIEGAV SSSDASTAKL
     KSYGIPVFDC NDVDVLDIYV DGADEINGQM QMIKGGGAAL TREKIIAAIA RKFICIADES
     KQVGVLGKFP LPVEVIPMAR SYVARELIKL GGLPEYRQNV LTDNGNVILD VHNLSILDAI
     ALENQINGIA GVVTVGLFAN RGADVALIGT ANGVKVIG
//

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