ID   Y402_RICCN              Reviewed;         144 AA.
AC   Q92IL8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Putative sugar phosphate isomerase RC0402;
DE            EC=5.3.1.-;
GN   OrderedLocusNames=RC0402;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
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DR   EMBL; AE006914; AAL02940.1; -; Genomic_DNA.
DR   PIR; B97750; B97750.
DR   RefSeq; WP_010977056.1; NC_003103.1.
DR   AlphaFoldDB; Q92IL8; -.
DR   SMR; Q92IL8; -.
DR   GeneID; 928667; -.
DR   KEGG; rco:RC0402; -.
DR   HOGENOM; CLU_091396_4_1_5; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR   InterPro; IPR004785; RpiB.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   NCBIfam; TIGR01120; rpiB; 1.
DR   NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR   PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1.
DR   PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1.
DR   Pfam; PF02502; LacAB_rpiB; 1.
DR   PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR   SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..144
FT                   /note="Putative sugar phosphate isomerase RC0402"
FT                   /id="PRO_0000269486"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   144 AA;  15907 MW;  BEAC8487BDE1C077 CRC64;
     MKTYNIVIAS DHSGYELKSE IINYLEQKSL KIYDCGTNNT QTVDYPDYAK KVVDIIIEKS
     APIGILISDT GIGMSIAANR SSEIRAALCN NILTAENAKA HNDANILILG AKTIDQKIVF
     DIIDKFLTTQ FEGGRHSTRL SKIK
//