ID   COFC_METAR              Reviewed;         219 AA.
AC   Q0W6V1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=UNCMA_22900;
GN   ORFNames=RCIX464;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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; AM114193; CAJ35892.1; -; Genomic_DNA.
DR   RefSeq; WP_012036610.1; NC_009464.1.
DR   AlphaFoldDB; Q0W6V1; -.
DR   SMR; Q0W6V1; -.
DR   STRING; 351160.RCIX464; -.
DR   EnsemblBacteria; CAJ35892; CAJ35892; RCIX464.
DR   GeneID; 5145593; -.
DR   KEGG; rci:RCIX464; -.
DR   eggNOG; arCOG04472; Archaea.
DR   OMA; FRVDYHG; -.
DR   OrthoDB; 67356at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000663; 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..219
FT                   /note="2-phospho-L-lactate guanylyltransferase"
FT                   /id="PRO_0000398763"
SQ   SEQUENCE   219 AA;  24107 MW;  C9B5A8DF2B54B260 CRC64;
     MKAIVPFKVV NVKSRLASLL TPEERSELAK LMLRDITSTL AAAGVEVELL TTQPFEWDGA
     TVIVSEKELN PALNDYLLAN DSPVMIVMAD IPLITEKNVR DMLASPADIV ICPGRGGGTN
     VQLIRRPDKY HVDYYGASFM DHMRIAQENG LTTEVFDSFN VSSDIDEAGD LIELYIHGKG
     DAAKYLRSIT VLDDSKGRVR VVKEESNLRA VRIPGKMTG