ID M0I006_9EURY Unreviewed; 206 AA.
AC M0I006;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=C441_14024 {ECO:0000313|EMBL:ELZ90031.1};
OS Haloferax sulfurifontis ATCC BAA-897.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=662480 {ECO:0000313|EMBL:ELZ90031.1, ECO:0000313|Proteomes:UP000011508};
RN [1] {ECO:0000313|EMBL:ELZ90031.1, ECO:0000313|Proteomes:UP000011508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-897 {ECO:0000313|EMBL:ELZ90031.1,
RC ECO:0000313|Proteomes:UP000011508};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ90031.1}.
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DR EMBL; AOLM01000023; ELZ90031.1; -; Genomic_DNA.
DR RefSeq; WP_007275609.1; NZ_AOLM01000023.1.
DR AlphaFoldDB; M0I006; -.
DR PATRIC; fig|662480.6.peg.2794; -.
DR OrthoDB; 11179at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000011508; 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 Gene3D; 6.10.140.50; -; 1.
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:ELZ90031.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:ELZ90031.1}.
SQ SEQUENCE 206 AA; 21693 MW; 1BA8BFD1FBC5635F CRC64;
MRVVVPFGGR EPKTRLASFF DADERREFAV SMLRDVLDAV RAAGGDPAVV ADAPVSVGAP
VTVDDRPLTA VVGDELDGLG GDPVAVVMAD LALATPAALA RLFETDGDVV AAPGLGGGTN
ALVVRDPKFS VDYHGASILD HRRIAREAGC SFAEVDSMRL AVDVDEPSDL VEVLVHGEGR
AREWLVDAGV RLERGTGRVE AVRARR
//
