ID   FBID_MYCRK              Reviewed;         221 AA.
AC   E5ASS2;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=3-phospho-D-glycerate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114, ECO:0000305};
DE            Short=3PG guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            EC=2.7.7.106 {ECO:0000255|HAMAP-Rule:MF_02114, ECO:0000269|PubMed:31469543};
GN   Name=cofC {ECO:0000303|PubMed:31469543};
GN   OrderedLocusNames=RBRH_02550 {ECO:0000312|EMBL:CBW75654.1};
OS   Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
OS   (Paraburkholderia rhizoxinica).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Mycetohabitans.
OX   NCBI_TaxID=882378;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19002 / CIP 109453 / HKI 454;
RX   PubMed=21131495; DOI=10.1128/jb.01318-10;
RA   Lackner G., Moebius N., Partida-Martinez L., Hertweck C.;
RT   "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont of
RT   Rhizopus microsporus.";
RL   J. Bacteriol. 193:783-784(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=31469543; DOI=10.1021/acschembio.9b00605;
RA   Braga D., Last D., Hasan M., Guo H., Leichnitz D., Uzum Z., Richter I.,
RA   Schalk F., Beemelmanns C., Hertweck C., Lackner G.;
RT   "Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-
RT   overlooked derivatives of coenzyme F420.";
RL   ACS Chem. Biol. 14:2088-2094(2019).
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       Can also use (2S)-2-phospholactate (2-PL), with lower turnover, and has
CC       weak activity with phosphoenolpyruvate (PEP).
CC       {ECO:0000269|PubMed:31469543}.
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         ECO:0000269|PubMed:31469543};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63441;
CC         Evidence={ECO:0000269|PubMed:31469543};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-
CC         5'-guanosine + diphosphate; Xref=Rhea:RHEA:63424, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:59435,
CC         ChEBI:CHEBI:59906; Evidence={ECO:0000269|PubMed:31469543};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63425;
CC         Evidence={ECO:0000269|PubMed:31469543};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02114, ECO:0000269|PubMed:31469543}.
CC   -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC       Rule:MF_02114}.
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DR   EMBL; FR687359; CBW75654.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5ASS2; -.
DR   SMR; E5ASS2; -.
DR   STRING; 882378.RBRH_02550; -.
DR   EnsemblBacteria; CBW75654; CBW75654; RBRH_02550.
DR   KEGG; brh:RBRH_02550; -.
DR   eggNOG; COG1920; Bacteria.
DR   HOGENOM; CLU_076569_1_0_4; -.
DR   OMA; HYDEDSY; -.
DR   BioCyc; MetaCyc:MON-21053; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000007437; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043814; F:phospholactate guanylyltransferase activity; IEA:InterPro.
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   1: Evidence at protein level;
KW   GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..221
FT                   /note="3-phospho-D-glycerate guanylyltransferase"
FT                   /id="PRO_0000452327"
SQ   SEQUENCE   221 AA;  23341 MW;  9395EF11EC2C2B73 CRC64;
     MRCNGMSPVS VAQRNTGIWA VVPLKAPECA KTRLSGVLSH AARQALFFSM ASHVIGTLRA
     SPRIASLLVV TPSESTAEMA RAAGAEILWG PPDEGMANAC SRAMAHIAAA GGERVMFVPG
     DLPLLDGAAI DMLSRAPVDA IGMAPNRDGH GTNGLICRPG AIPLFFSGPS FSAHQNAARC
     AGIDVWIVRS REWALDVDLP ADLEEFESSI KDAKRRVLCQ I