ID   COFD_HALMA              Reviewed;         330 AA.
AC   Q5V5R9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=rrnAC0051;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV45133.1; -; Genomic_DNA.
DR   RefSeq; WP_007188235.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V5R9; -.
DR   SMR; Q5V5R9; -.
DR   STRING; 272569.rrnAC0051; -.
DR   EnsemblBacteria; AAV45133; AAV45133; rrnAC0051.
DR   GeneID; 40154366; -.
DR   KEGG; hma:rrnAC0051; -.
DR   PATRIC; fig|272569.17.peg.861; -.
DR   eggNOG; arCOG04395; Archaea.
DR   HOGENOM; CLU_055795_1_0_2; -.
DR   OMA; DLDTVMY; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001169; Chromosome I.
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   Gene3D; 3.40.50.10680; -; 2.
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..330
FT                   /note="2-phospho-L-lactate transferase"
FT                   /id="PRO_0000145769"
FT   BINDING         49
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   330 AA;  35021 MW;  4AD230ADF366262B CRC64;
     MVTFLAGGTG TPKLLAGADD VFSPAATTVV ANTGDDIELG GHLVCPDLDT VLFLDGEVLD
     RETWWGIADD TAETHTELTR LADAAGLDGG PRYLPDDAQT AGRDIARWRR FSGVAEFMHI
     GDRDRAVHVT RTSLLDEGRS LTAVTRTLAD AFGLERTLLP MSDDPVASII HTPSGPMHFQ
     EWWVGRNGEP PVEDVEFRGA ERASATDAVL TALDDTVVIG PSNPVTSLGP MLAIDDIQRA
     LHETTVVAVS PFIEDTVFSG PAADLMAGVG LEPSTAGVAE AYPFADSFVL DEEDSTPLDV
     PVVRTDTTLN DAADAERVNR AVETALSEVA