ID   COFC_HALSA              Reviewed;         209 AA.
AC   Q9HNV0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=VNG_1935C;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG20120.1; -; Genomic_DNA.
DR   PIR; D84344; D84344.
DR   RefSeq; WP_010903420.1; NC_002607.1.
DR   AlphaFoldDB; Q9HNV0; -.
DR   SMR; Q9HNV0; -.
DR   STRING; 64091.VNG_1935C; -.
DR   PaxDb; Q9HNV0; -.
DR   EnsemblBacteria; AAG20120; AAG20120; VNG_1935C.
DR   GeneID; 5953169; -.
DR   GeneID; 62887278; -.
DR   KEGG; hal:VNG_1935C; -.
DR   PATRIC; fig|64091.14.peg.1479; -.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   InParanoid; Q9HNV0; -.
DR   OMA; FRVDYHG; -.
DR   OrthoDB; 67356at2157; -.
DR   PhylomeDB; Q9HNV0; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043814; F:phospholactate guanylyltransferase activity; IBA:GO_Central.
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..209
FT                   /note="2-phospho-L-lactate guanylyltransferase"
FT                   /id="PRO_0000398726"
SQ   SEQUENCE   209 AA;  21875 MW;  2D83C5960119CD1F CRC64;
     MRTVVPFDPR DPKSRLAEFF ADAEERRGFA YAMLADVLGA VRDAGGDPVV VATAPVSRPV
     DAPVTVDDRA LSTAVAAAIA DGPLPTAVVM ADLALATPDA IRRVFAASGD VVLAPGSGGG
     TNVVLARTAD VPVSYHGVSF RDHVTAAERA GLTVTTVDSF RLAADVDDAS DLVDVFVHNT
     RRTREWLIAG GWRLAVDDGT PTVVREPND