COFC_METSF
ID COFC_METSF Reviewed; 227 AA.
AC D3S534;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 25-MAY-2022, entry version 54.
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};
GN OrderedLocusNames=MFS40622_1271;
OS Methanocaldococcus sp. (strain FS406-22).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus; unclassified Methanocaldococcus.
OX NCBI_TaxID=644281;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS406-22;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Leigh J.,
RA Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.";
RL Submitted (FEB-2010) 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; CP001901; ADC69948.1; -; Genomic_DNA.
DR RefSeq; WP_012980856.1; NC_013887.1.
DR AlphaFoldDB; D3S534; -.
DR SMR; D3S534; -.
DR STRING; 644281.MFS40622_1271; -.
DR EnsemblBacteria; ADC69948; ADC69948; MFS40622_1271.
DR GeneID; 8805130; -.
DR KEGG; mfs:MFS40622_1271; -.
DR eggNOG; arCOG04472; Archaea.
DR HOGENOM; CLU_076569_2_0_2; -.
DR OMA; FRVDYHG; -.
DR OrthoDB; 67356at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000002189; 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..227
FT /note="2-phospho-L-lactate guanylyltransferase"
FT /id="PRO_0000398739"
SQ SEQUENCE 227 AA; 25888 MW; E53D1B281964CF02 CRC64;
MKVLIPVSPI NSLKTRLSEF LSSEERKNLL LNMLRDINKA LEGLDVVIIS RDEEILEFGK
NELKAETIKE KYKGLNKAIK QAFEEIEDDE VIIIPADIPL IKKRHIEDIL KLSKDYDVII
APSRGGGTNL LYLKSKNLIE IKYEGFSFLK HLEEAKKKNL RYYIYDSFLI SVDINTPEDL
GEIFIHGDST YTKNYLKGLG IEVESKHSSA GRFVVKRGGD NEVSNPM