ID A0A166E0J5_9EURY Unreviewed; 223 AA.
AC A0A166E0J5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=2-phospho-L-lactate guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE Short=LP guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE EC=2.7.7.68 {ECO:0000256|HAMAP-Rule:MF_02114};
GN Name=cofC {ECO:0000256|HAMAP-Rule:MF_02114,
GN ECO:0000313|EMBL:KZX16146.1};
GN ORFNames=MBCUT_10120 {ECO:0000313|EMBL:KZX16146.1};
OS Methanobrevibacter cuticularis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX16146.1, ECO:0000313|Proteomes:UP000077275};
RN [1] {ECO:0000313|EMBL:KZX16146.1, ECO:0000313|Proteomes:UP000077275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX16146.1,
RC ECO:0000313|Proteomes:UP000077275};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL Submitted (APR-2016) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_02114};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02114}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02114}.
CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000256|HAMAP-
CC Rule:MF_02114}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZX16146.1}.
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DR EMBL; LWMW01000098; KZX16146.1; -; Genomic_DNA.
DR RefSeq; WP_067259608.1; NZ_LWMW01000098.1.
DR AlphaFoldDB; A0A166E0J5; -.
DR STRING; 47311.MBCUT_10120; -.
DR PATRIC; fig|47311.3.peg.1115; -.
DR OrthoDB; 11179at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000077275; Unassembled WGS sequence.
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 HAMAP; MF_02114; CofC; 1.
DR InterPro; IPR002835; CofC.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR03552; F420_cofC; 1.
DR PANTHER; PTHR40392; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR PANTHER; PTHR40392:SF1; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR Pfam; PF01983; CofC; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_02114,
KW ECO:0000313|EMBL:KZX16146.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077275};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:KZX16146.1}.
SQ SEQUENCE 223 AA; 24921 MW; E25585C0684F768A CRC64;
MDEIYGIIPV SKFSNAKTRL SPFLDLEERE KLLKAMLKDV VSTLKPVVDE VIIISADKDV
LEYANDLEVL TLVENEGLYL NTAIAQAMDW CRHKTEKVII IPSDIPLIAK TNLQPLIESA
KALDFIICPS KGGGTNGLLI NPLAIDMKFG DFSFMKHINE AKNKGLDPIV YDSFYISLDV
NITEDIGEIM IHGDGTKTKN YLNSLNIEVE SIHGTERLKI TRK
//