ID   CPGS_RUBXD              Reviewed;         442 AA.
AC   Q1AVG0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Cyclic 2,3-diphosphoglycerate synthetase {ECO:0000255|HAMAP-Rule:MF_01908};
DE            Short=cDPGS {ECO:0000255|HAMAP-Rule:MF_01908};
DE            EC=6.5.1.9 {ECO:0000255|HAMAP-Rule:MF_01908};
GN   Name=cpgS {ECO:0000255|HAMAP-Rule:MF_01908}; OrderedLocusNames=Rxyl_1657;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of cyclic 2,3-diphosphoglycerate
CC       (cDPG) by formation of an intramolecular phosphoanhydride bond at the
CC       expense of ATP. {ECO:0000255|HAMAP-Rule:MF_01908}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-
CC         2,3-bisphosphoglycerate + phosphate; Xref=Rhea:RHEA:42412,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58248, ChEBI:CHEBI:79081, ChEBI:CHEBI:456216; EC=6.5.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01908};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01908}.
CC   -!- SIMILARITY: Belongs to the cyclic 2,3-diphosphoglycerate synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01908}.
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DR   EMBL; CP000386; ABG04618.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1AVG0; -.
DR   STRING; 266117.Rxyl_1657; -.
DR   EnsemblBacteria; ABG04618; ABG04618; Rxyl_1657.
DR   KEGG; rxy:Rxyl_1657; -.
DR   eggNOG; COG2403; Bacteria.
DR   HOGENOM; CLU_638764_0_0_11; -.
DR   OMA; RRCGGGM; -.
DR   PhylomeDB; Q1AVG0; -.
DR   Proteomes; UP000006637; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0036356; F:cyclic 2,3-diphosphoglycerate synthetase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   HAMAP; MF_01908; Cyc_PG_syn; 1.
DR   InterPro; IPR016557; Cyc_diphosphoglycerate_synth.
DR   PIRSF; PIRSF009445; Cyc_PG_syn; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..442
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_0000313688"
SQ   SEQUENCE   442 AA;  47038 MW;  66A18168B15375FD CRC64;
     MRTLFLIDGE HYPPVVLDAM RRVREQLGAK GVAAAFLGGT EKIGEGADYG LPLVAAEDPV
     SAVRQALERY GVEAVVDLSD EPVVGYRERM RIASLALAAG ARYVGSDFEL RPPEMRRVPG
     KPSLAVIGTG KRVGKTAVTG YLARLLDREG FRPAVVSMGR GGPPEPEVLE GRRLEVGSDY
     LLRALERGAH AASDYYETAA LSRVTTVGCR RCGGGLAGEP FVSNVLEGAR IAAGLDTGIT
     VFDGSGAAIP PVEVDRRVLV AGAHQDPEYV AGYLGAYRLL ISDLLVLTMA EEPMAPPGRV
     EELVRRVREV RPDLPVIPAV FRPRPVGEVR GMRVAYVSTA PPAVLKRLAG HLEEGYGCEV
     VAVSGNLSNR SKLAEDLEGM PGVDAYLTEI KAAAVDVVTR RGAEEGRRVI YCDNDPVAEG
     LDGALLRLAR AAGRGRSGDR GV