ID   COFC_METRM              Reviewed;         234 AA.
AC   D3E2P3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 56.
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=mru_0953;
OS   Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS   OCM 146 / M1) (Methanobacterium ruminantium).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=634498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1;
RX   PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA   Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA   Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA   Janssen P.H., Dey D., Attwood G.T.;
RT   "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT   reveals new possibilities for controlling ruminant methane emissions.";
RL   PLoS ONE 5:E8926-E8926(2010).
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; CP001719; ADC46804.1; -; Genomic_DNA.
DR   RefSeq; WP_012955755.1; NC_013790.1.
DR   AlphaFoldDB; D3E2P3; -.
DR   SMR; D3E2P3; -.
DR   STRING; 634498.mru_0953; -.
DR   EnsemblBacteria; ADC46804; ADC46804; mru_0953.
DR   GeneID; 8770605; -.
DR   KEGG; mru:mru_0953; -.
DR   PATRIC; fig|634498.28.peg.955; -.
DR   eggNOG; arCOG04472; Archaea.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   OMA; FRVDYHG; -.
DR   OrthoDB; 67356at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000008680; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..234
FT                   /note="2-phospho-L-lactate guanylyltransferase"
FT                   /id="PRO_0000398735"
SQ   SEQUENCE   234 AA;  26592 MW;  46EFA283C6040880 CRC64;
     MDKIYAIIPV NQFANAKTRL SPFLTPEERR DLLKAMLKDI TDTLKPIVDK VVIISRDEEV
     LAYAEELELT TIVEEEYKKS KAVNSSDDNP LNKALKQAMK WSRKKTRKVI ILPSDIPLIG
     KTNVKLLIDQ AKNFDFIIVP SKGGGTNTLI IKPLAIDMKF EGFSFNKHIE EAKRKKLVPI
     VHDSFYMALD VNTTEDLGEI MLHGNGTETK KYLESLGIKV ESSHDHERLK VTRD