ID   COFD_METBF              Reviewed;         309 AA.
AC   Q46C16;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Mbar_A1631;
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: 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; CP000099; AAZ70576.1; -; Genomic_DNA.
DR   RefSeq; WP_011306622.1; NC_007355.1.
DR   AlphaFoldDB; Q46C16; -.
DR   SMR; Q46C16; -.
DR   STRING; 269797.Mbar_A1631; -.
DR   EnsemblBacteria; AAZ70576; AAZ70576; Mbar_A1631.
DR   GeneID; 3627330; -.
DR   KEGG; mba:Mbar_A1631; -.
DR   eggNOG; arCOG04395; Archaea.
DR   HOGENOM; CLU_055795_1_0_2; -.
DR   OMA; DLDTVMY; -.
DR   OrthoDB; 31831at2157; -.
DR   UniPathway; UPA00071; -.
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_0000259479"
FT   BINDING         48
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         87
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;  33766 MW;  B326BA05C41CEB17 CRC64;
     MIIFSGGTGT PKLLDGLKEI LPAEEMTVVV NTAEDLWVSG NLICPDLDTV IYLFSDQIDR
     NRWWGVKDDT FLTYERMQKL GVMESMKLGD CDRATHIIRS NFIRSGISLT DAILELASIF
     GIDAKILPMS DDPVSTYIEA PEAILHFQDF WIGKHGEPEV LGVDITGISE ASISPKVLEA
     LENDDNVLIG PSNPITSIGP IISLPGMKDL LKKKKVVAVS PIIGNAPVSG PAGKLMKACG
     LEVSSMGVAE YYQDFLDIFV FDERDQADEF AFEKLGCRAS RADTLMTSTE KSKELAELVV
     GLFDTIVCP