COFC_METBF
ID COFC_METBF Reviewed; 208 AA.
AC Q466A1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Mbar_A3418;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(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; CP000099; AAZ72291.1; -; Genomic_DNA.
DR RefSeq; WP_011308330.1; NC_007355.1.
DR AlphaFoldDB; Q466A1; -.
DR SMR; Q466A1; -.
DR STRING; 269797.Mbar_A3418; -.
DR EnsemblBacteria; AAZ72291; AAZ72291; Mbar_A3418.
DR GeneID; 3624705; -.
DR KEGG; mba:Mbar_A3418; -.
DR eggNOG; arCOG04472; Archaea.
DR HOGENOM; CLU_076569_2_0_2; -.
DR OMA; FRVDYHG; -.
DR OrthoDB; 67356at2157; -.
DR UniPathway; UPA00071; -.
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..208
FT /note="2-phospho-L-lactate guanylyltransferase"
FT /id="PRO_0000398756"
SQ SEQUENCE 208 AA; 22916 MW; 4AE443D9E6BE9B94 CRC64;
MKAVIPYKKS SAKSRLSPVL TREEREEFVD LMLNQVIDTL KEAGVGTIDI LSPSMYGLEN
MTKANVLLDK NDLNEALNGY LEQAEEPVII VMADLPLLSP DHVKGITSTK EDVCIVPGKG
GGTNALFIKN PSCYRVRYYG SSFLTHCSIA EKTGQSVEVY DSFFAGTDID EPEDLVELLI
HGSGAAKEYI SKKFRLEMSR GRVGLVHI