ID   COFD_METKA              Reviewed;         310 AA.
AC   Q8TVA3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=MK1489;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02702.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TVA3; -.
DR   SMR; Q8TVA3; -.
DR   STRING; 190192.MK1489; -.
DR   EnsemblBacteria; AAM02702; AAM02702; MK1489.
DR   KEGG; mka:MK1489; -.
DR   PATRIC; fig|190192.8.peg.1647; -.
DR   HOGENOM; CLU_055795_1_0_2; -.
DR   OMA; DLDTVMY; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001826; 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; Reference proteome; Transferase.
FT   CHAIN           1..310
FT                   /note="2-phospho-L-lactate transferase"
FT                   /id="PRO_0000145773"
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   310 AA;  34882 MW;  1EA80A7C3DCD8975 CRC64;
     MNLRLTVLSG GTGTPKLLRG LRELEADFSV IVNTGEDDEI LGLYVSPDVD TVLYTLAGIV
     NDETWYGIKD DGFRGHEFLE RLGVDEPLRI GDADRALKQY RTYLMREKGL KLSEAVDEIR
     RRLGIKWKVY PMTDDRVTTI VETDEGDLHF REFWVERGGK PPVRGVRYEG AEEASPPPDA
     VDELLRADVV LIGPSNPVTS IGPILSISEI RHIVREKPVV MVSPFIGREP VSGPAGKLMR
     AVGFEPSVRG LVEYYREWGV EPDVLIMDER DDVELPEGLE VVRTDTLMRD EKDSVRLARE
     VLRIVEELVG