ID   FBID_AFIC5              Reviewed;         237 AA.
AC   B6JBS5; F8BXW4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=3-phospho-D-glycerate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            Short=3PG guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            EC=2.7.7.106 {ECO:0000255|HAMAP-Rule:MF_02114};
GN   Name=fbiD {ECO:0000255|HAMAP-Rule:MF_02114};
GN   OrderedLocusNames=OCAR_5006, OCA5_c29520;
OS   Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS   (Oligotropha carboxidovorans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Afipia.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=18539730; DOI=10.1128/jb.00614-08;
RA   Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT   "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT   carboxidovorans OM5T.";
RL   J. Bacteriol. 190:5531-5532(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/jb.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
CC   -!- FUNCTION: Guanylyltransferase that catalyzes the activation of (2R)-3-
CC       phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via
CC       the condensation of 3PG with GTP. It is involved in the biosynthesis of
CC       a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420.
CC       {ECO:0000255|HAMAP-Rule:MF_02114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + GTP + H(+) = 3-[(R)-glyceryl]-
CC         diphospho-5'-guanosine + diphosphate; Xref=Rhea:RHEA:63440,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58272, ChEBI:CHEBI:147306; EC=2.7.7.106;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02114};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02114}.
CC   -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC       Rule:MF_02114}.
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DR   EMBL; CP001196; ACI92141.1; -; Genomic_DNA.
DR   EMBL; CP002826; AEI07643.1; -; Genomic_DNA.
DR   RefSeq; WP_012562171.1; NC_015684.1.
DR   AlphaFoldDB; B6JBS5; -.
DR   SMR; B6JBS5; -.
DR   STRING; 504832.OCAR_5006; -.
DR   EnsemblBacteria; AEI07643; AEI07643; OCA5_c29520.
DR   KEGG; oca:OCAR_5006; -.
DR   KEGG; ocg:OCA5_c29520; -.
DR   eggNOG; COG1920; Bacteria.
DR   HOGENOM; CLU_076569_1_0_5; -.
DR   OMA; RCDIDTP; -.
DR   OrthoDB; 1930370at2; -.
DR   BRENDA; 2.7.7.106; 4399.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000007730; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043814; F:phospholactate guanylyltransferase activity; IEA:InterPro.
DR   GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_02114; CofC; 1.
DR   InterPro; IPR002835; CofC.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR40392; PTHR40392; 1.
DR   Pfam; PF01983; CofC; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03552; F420_cofC; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..237
FT                   /note="3-phospho-D-glycerate guanylyltransferase"
FT                   /id="PRO_0000398703"
SQ   SEQUENCE   237 AA;  24729 MW;  86386D22165D9194 CRC64;
     MARSDAFVIL PVKAFVGAKS RLAPLLSVGE RTMLARVMLN DVLDAAIAAV GPQSVSVVTS
     ADDVADHARR AGVGVIDDEG ARGTNAAVKV GFARIAARRR GAVLTLSSDI PGLIPSDIVA
     LISAAERSRV ALAPACDDGG TNALACDVVG RIPLCFGPGS FARHIAAANA ADVRPAVLLN
     QRLGLDLDEP HHLMQFLDRG TSTQTDAYLR VLRLKERKGH SFVVAAQQAT GARRLAV