ID   COFD_METM5              Reviewed;         309 AA.
AC   A4FZ98;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=2-phospho-L-lactate transferase {ECO:0000255|HAMAP-Rule:MF_01257};
DE            EC=2.7.8.28 {ECO:0000255|HAMAP-Rule:MF_01257};
GN   Name=cofD {ECO:0000255|HAMAP-Rule:MF_01257}; OrderedLocusNames=MmarC5_1234;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of the 2-phospholactate moiety from
CC       (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-
CC       deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and
CC       GMP. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-
CC         hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0;
CC         Xref=Rhea:RHEA:63444, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:59435, ChEBI:CHEBI:59904, ChEBI:CHEBI:59907; EC=2.7.8.28;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01257};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01257};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- SIMILARITY: Belongs to the CofD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01257}.
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DR   EMBL; CP000609; ABO35532.1; -; Genomic_DNA.
DR   RefSeq; WP_011868985.1; NC_009135.1.
DR   AlphaFoldDB; A4FZ98; -.
DR   SMR; A4FZ98; -.
DR   STRING; 402880.MmarC5_1234; -.
DR   EnsemblBacteria; ABO35532; ABO35532; MmarC5_1234.
DR   GeneID; 4929043; -.
DR   KEGG; mmq:MmarC5_1234; -.
DR   eggNOG; arCOG04395; Archaea.
DR   HOGENOM; CLU_055795_1_0_2; -.
DR   OMA; DLDTVMY; -.
DR   OrthoDB; 31831at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000253; Chromosome.
DR   GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07186; CofD_like; 1.
DR   Gene3D; 3.40.50.10680; -; 1.
DR   HAMAP; MF_01257; CofD; 1.
DR   InterPro; IPR002882; CofD.
DR   InterPro; IPR038136; CofD-like_dom_sf.
DR   InterPro; IPR010115; FbiA/CofD.
DR   PANTHER; PTHR43007; PTHR43007; 1.
DR   Pfam; PF01933; CofD; 1.
DR   SUPFAM; SSF142338; SSF142338; 1.
DR   TIGRFAMs; TIGR01819; F420_cofD; 1.
PE   3: Inferred from homology;
KW   Magnesium; Transferase.
FT   CHAIN           1..309
FT                   /note="2-phospho-L-lactate transferase"
FT                   /id="PRO_1000067246"
FT   BINDING         50
FT                   /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT                   /ligand_id="ChEBI:CHEBI:59904"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01257"
FT   BINDING         89
FT                   /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT                   /ligand_id="ChEBI:CHEBI:59904"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01257"
SQ   SEQUENCE   309 AA;  34552 MW;  A021F3AE2BCB5E22 CRC64;
     MNITILSGGT GTPKLIQGFK EIIPNEDISV IVNTGEDTYI GDIYLSPDID TVLYTFSDLI
     NDETWYGLKG DTFICHEQLK KFGFDEVLKI GDKDRALKMH KASSLKNGVP MSEIVDIERK
     SLSLKSKIYP MSNERVESKV LIEENNEKIL LKFHDFWIFR KGNAKVLDIF YENSNYAKAA
     DGVIKAIEES DFILIGPSNP ITSIGPILSI SEIKNALKEK LVFAVSPIVG ENPVSGPAGT
     LMNAKGYPVS AVGVYEYYKD IVDVLVLDNS DINKKKDINC EVLYANTIMK TIDDKITLAR
     NILDYYKSR