COFD_METLZ
ID COFD_METLZ Reviewed; 304 AA.
AC A2SPS3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Mlab_0152;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06329.1; -; Genomic_DNA.
DR RefSeq; WP_011832530.1; NC_008942.1.
DR AlphaFoldDB; A2SPS3; -.
DR SMR; A2SPS3; -.
DR STRING; 410358.Mlab_0152; -.
DR EnsemblBacteria; ABN06329; ABN06329; Mlab_0152.
DR GeneID; 4795986; -.
DR KEGG; mla:Mlab_0152; -.
DR eggNOG; arCOG04395; Archaea.
DR HOGENOM; CLU_055795_1_0_2; -.
DR OMA; DLDTVMY; -.
DR OrthoDB; 31831at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000365; 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..304
FT /note="2-phospho-L-lactate transferase"
FT /id="PRO_1000165109"
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 304 AA; 33547 MW; 21C2F2813EA3E6B2 CRC64;
MITVFSGGTG TPKLIRGLRQ ILHDHEITVV VNTAEDLWMS GLYVSPDIDT VQYLFSGLLN
TDSWWGIRGD SFETFHAMEK LGYTELLPLG DKDRATNIAR AEFLRQGMTL TEATEKIAKG
YGVSARILPM SDQNVASYVV CEDDSLMHYQ EYWVGKRGNV NIKGVVRKTT DGLPLKTTPE
VISAIEESDG VIIGPSNPVT SIGPILECAG VREALQNTFT AAVSPFIGNR PVSGPAAALM
KAWGYESTSY GTWQVYKDVV DLFIQDVRDT AIEVPGAHRL DTMMTNEKKA ESLAWDLLSY
FPRK