COFC_METLZ
ID COFC_METLZ Reviewed; 212 AA.
AC A2ST69;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, 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=Mlab_1358;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN07525.1; -; Genomic_DNA.
DR RefSeq; WP_011833728.1; NC_008942.1.
DR AlphaFoldDB; A2ST69; -.
DR SMR; A2ST69; -.
DR STRING; 410358.Mlab_1358; -.
DR PRIDE; A2ST69; -.
DR EnsemblBacteria; ABN07525; ABN07525; Mlab_1358.
DR GeneID; 4795349; -.
DR KEGG; mla:Mlab_1358; -.
DR eggNOG; arCOG04472; Archaea.
DR HOGENOM; CLU_076569_2_0_2; -.
DR OMA; FRVDYHG; -.
DR OrthoDB; 67356at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000365; 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..212
FT /note="2-phospho-L-lactate guanylyltransferase"
FT /id="PRO_0000398749"
SQ SEQUENCE 212 AA; 23969 MW; 99150DEA8F38D23E CRC64;
MYFHALIPFK PVNPKTRLSS VLSQEEREEF ARIMLEDVIL AVRRTGCSAT LLCTSKYECR
DALVAIRKEG LNEAINWALP QFHCPALIIM SDLPMVTPGS LQRVISTKAD MAIVPGLGGG
TNVIFVKKPE KFHVEYYGFS FRRHLQIAEE LELTVEIIDS MRMSTDVDEP ADLVELMIHG
HGNAREWLYE HGFSLSVEDG RVKVHRDGKE VV