ID   FBID_PHEZH              Reviewed;         218 AA.
AC   B4RGP0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
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}; OrderedLocusNames=PHZ_c2537;
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1;
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000747; ACG78946.1; -; Genomic_DNA.
DR   RefSeq; WP_012523084.1; NC_011144.1.
DR   AlphaFoldDB; B4RGP0; -.
DR   SMR; B4RGP0; -.
DR   STRING; 450851.PHZ_c2537; -.
DR   EnsemblBacteria; ACG78946; ACG78946; PHZ_c2537.
DR   KEGG; pzu:PHZ_c2537; -.
DR   eggNOG; COG1920; Bacteria.
DR   HOGENOM; CLU_076569_1_0_5; -.
DR   OMA; RCDIDTP; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001868; 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..218
FT                   /note="3-phospho-D-glycerate guanylyltransferase"
FT                   /id="PRO_0000398704"
SQ   SEQUENCE   218 AA;  22786 MW;  2CED591674938AEA CRC64;
     MAEAILAVRG GLGAKSRLAA VFSDAERAAL VEAMLLDMLD ALAGAGAGAV RRVWVVTPTE
     RLERLAAAAG ARVIREPRPA GLNAAFRCGL AAAAEEAPYA DIVLLPGDLP TLRAQDVDAA
     LLLLRTHDLV LALASRDGGT GLLAVRAGVP FTPQFGAQSC ARHRRQARAR GLSCALVEAG
     SLALDLDRPE DAVEVARGPC GRRTAEVLSD LKSRWRAQ