ID   COFC_METFA              Reviewed;         218 AA.
AC   C7P592;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=2-phospho-L-lactate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            Short=LP guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            EC=2.7.7.68 {ECO:0000255|HAMAP-Rule:MF_02114};
GN   Name=cofC {ECO:0000255|HAMAP-Rule:MF_02114}; OrderedLocusNames=Mefer_1466;
OS   Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)
OS   (Methanococcus fervens).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573064;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4213 / JCM 15782 / AG86;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lupa-Sieprawska M., Whitman W.B.;
RT   "Complete sequence of chromosome of Methanocaldococcus fervens AG86.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanylyltransferase that catalyzes the activation of (2S)-2-
CC       phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the
CC       condensation of 2-PL with GTP. It is involved in the biosynthesis of
CC       coenzyme F420, a hydride carrier cofactor. {ECO:0000255|HAMAP-
CC       Rule:MF_02114}.
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; EC=2.7.7.68; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02114};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02114}.
CC   -!- SUBUNIT: Homodimer. {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; CP001696; ACV25270.1; -; Genomic_DNA.
DR   RefSeq; WP_015792003.1; NC_013156.1.
DR   AlphaFoldDB; C7P592; -.
DR   SMR; C7P592; -.
DR   STRING; 573064.Mefer_1466; -.
DR   EnsemblBacteria; ACV25270; ACV25270; Mefer_1466.
DR   GeneID; 8366172; -.
DR   KEGG; mfe:Mefer_1466; -.
DR   eggNOG; arCOG04472; Archaea.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   OMA; FRVDYHG; -.
DR   OrthoDB; 67356at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001495; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043814; F:phospholactate guanylyltransferase activity; IEA:UniProtKB-EC.
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; Transferase.
FT   CHAIN           1..218
FT                   /note="2-phospho-L-lactate guanylyltransferase"
FT                   /id="PRO_0000398737"
SQ   SEQUENCE   218 AA;  25104 MW;  221FE8C5A1BC52B4 CRC64;
     MKVIIPVSPI NSLKTRLSEF LSSEERKNLL LNMLRDIKKA LEGLDVVVVS RDDEILDFAK
     YELKAEIVKE KYKGLNNAIK QAFDEIDDEE VIIIPADIPL IKKKHIEDIL KLSKDYDLII
     ASSRGGGTNL LYLKSKNLIE LRYEGFSFLK HLEEAEKRNL RYYIYDSFLI SVDINTPEDL
     GEIFIHGDNT YTKNYLKGLG IEVEPKHSSA GRFVVKRR