ID   COFC_METS3              Reviewed;         224 AA.
AC   A5UJW5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Msm_0288;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86493.1; -; Genomic_DNA.
DR   RefSeq; WP_011953806.1; NC_009515.1.
DR   AlphaFoldDB; A5UJW5; -.
DR   SMR; A5UJW5; -.
DR   STRING; 420247.Msm_0288; -.
DR   EnsemblBacteria; ABQ86493; ABQ86493; Msm_0288.
DR   GeneID; 5216642; -.
DR   KEGG; msi:Msm_0288; -.
DR   PATRIC; fig|420247.28.peg.291; -.
DR   eggNOG; arCOG04472; Archaea.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   OMA; FRVDYHG; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001992; 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..224
FT                   /note="2-phospho-L-lactate guanylyltransferase"
FT                   /id="PRO_0000398736"
SQ   SEQUENCE   224 AA;  25346 MW;  F343B81C3F93B296 CRC64;
     MDDIYGIIPV SKFKECKTRL SPFLSEEERE NLLKVMLKDV TDTLRKYTDK IIIISADEDV
     LNYAKSLNLS VLKENDNSNL NKALKQAMEY CKGKTKKVII MPSDIPLIGK TNLKMVIDSS
     KQLDFIIIPS KGGGTNTIIM KPLAIRTKFG DFSYKEHVNA ADRKNLNPQV HDSLFMALDV
     NTTEDLGEII VHGENTETRR YLKELKINVE SVHGSERLKV TRGS