COFD_HALS3
ID COFD_HALS3 Reviewed; 336 AA.
AC B0R5L0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=OE_3057F;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774415; CAP14027.1; -; Genomic_DNA.
DR RefSeq; WP_010903040.1; NC_010364.1.
DR AlphaFoldDB; B0R5L0; -.
DR SMR; B0R5L0; -.
DR EnsemblBacteria; CAP14027; CAP14027; OE_3057F.
DR GeneID; 5952972; -.
DR KEGG; hsl:OE_3057F; -.
DR HOGENOM; CLU_055795_1_0_2; -.
DR OMA; DLDTVMY; -.
DR PhylomeDB; B0R5L0; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001321; 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; -; 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; Transferase.
FT CHAIN 1..336
FT /note="2-phospho-L-lactate transferase"
FT /id="PRO_1000139979"
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 336 AA; 35468 MW; C0486EE0726BB7CD CRC64;
MTTFLAGGTG TPKLLAGARR VFDPAETTVV GNTGDDVALG GLLVCPDLDT VLFEGGGVLD
RETWWGIADD GSTTHDYLTD LAAAADIDPD TPRYLPDDAQ TAGRDIARWR RFSAASEFMF
IGDRDRAVHT LRAGLLDEGH TLTEVTRRLA DAFDLSVDLV PMSNDPVATI VQTPDGEQHF
QTFWVAEHGD PTVEDVEFRG GERATAAQPA IEAIRDGPVV VGPSNPVTSI GPMLALDGIA
DALRDAQVVA VSPFVEDEVF SGPAAKLMAA VGHDPSTAGV ADAYDFADAF VLDTADSTDL
DRPVVRTDTS LDTEADAERV ARACRDALVA ASGEVT
