COFD_METJA
ID COFD_METJA Reviewed; 311 AA.
AC Q58653;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=2-phospho-L-lactate transferase {ECO:0000255|HAMAP-Rule:MF_01257, ECO:0000303|PubMed:11888293};
DE EC=2.7.8.28 {ECO:0000255|HAMAP-Rule:MF_01257};
DE AltName: Full=LPPG:FO 2-phospho-L-lactate transferase {ECO:0000303|PubMed:11888293};
GN Name=cofD {ECO:0000303|PubMed:11888293}; OrderedLocusNames=MJ1256;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MUTAGENESIS OF SER-211.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=11888293; DOI=10.1021/bi011937v;
RA Graupner M., Xu H., White R.H.;
RT "Characterization of the 2-phospho-L-lactate transferase enzyme involved in
RT coenzyme F(420) biosynthesis in Methanococcus jannaschii.";
RL Biochemistry 41:3754-3761(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, ECO:0000269|PubMed:11888293}.
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 ECO:0000269|PubMed:11888293};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11888293};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:11888293}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32 uM for FO {ECO:0000269|PubMed:11888293};
CC KM=17 uM for LPPG {ECO:0000269|PubMed:11888293};
CC KM=515 uM for LPPA {ECO:0000269|PubMed:11888293};
CC Vmax=1.4 umol/min/mg enzyme with LPPG as substrate
CC {ECO:0000269|PubMed:11888293};
CC Vmax=0.1 umol/min/mg enzyme with LPPA as substrate
CC {ECO:0000269|PubMed:11888293};
CC Temperature dependence:
CC Optimum temperature is about 37 degrees Celsius. Thermostable. Still
CC fully active after heating at 80 degrees Celsius for 24 hours.
CC Activity begins to decrease after heating at 98 degrees Celsius for
CC 30 minutes. Inactive after heating at 110 degrees Celsius for 30
CC minutes.;
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11888293}.
CC -!- SIMILARITY: Belongs to the CofD family. {ECO:0000305}.
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DR EMBL; L77117; AAB99260.1; -; Genomic_DNA.
DR PIR; G64456; G64456.
DR RefSeq; WP_010870769.1; NC_000909.1.
DR AlphaFoldDB; Q58653; -.
DR SMR; Q58653; -.
DR STRING; 243232.MJ_1256; -.
DR EnsemblBacteria; AAB99260; AAB99260; MJ_1256.
DR GeneID; 1452154; -.
DR KEGG; mja:MJ_1256; -.
DR eggNOG; arCOG04395; Archaea.
DR HOGENOM; CLU_055795_1_0_2; -.
DR InParanoid; Q58653; -.
DR OMA; DLDTVMY; -.
DR OrthoDB; 31831at2157; -.
DR PhylomeDB; Q58653; -.
DR BioCyc; MetaCyc:MON-12181; -.
DR BRENDA; 2.7.8.28; 3260.
DR SABIO-RK; Q58653; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IDA:MENGO.
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 1: Evidence at protein level;
KW Magnesium; Reference proteome; Transferase.
FT CHAIN 1..311
FT /note="2-phospho-L-lactate transferase"
FT /id="PRO_0000145772"
FT BINDING 52
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 91
FT /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT /ligand_id="ChEBI:CHEBI:59904"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01257"
FT MUTAGEN 211
FT /note="S->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:11888293"
SQ SEQUENCE 311 AA; 34599 MW; A2830E42C824F64F CRC64;
MIFVITVLSG GTGTPKLLQG LKRVVNNEEL AVIVNTGEDT WIGDLYLSPD VDTVLYTLAD
LINEETWYGV KEDTFYTHEQ LKNLGFDEVL RIGDKDRALK MHKTYYLKRG HKLSEVVDME
KVALGIKAKV IPMTDDRVET KILAKVDGKV DLLKFHDFWV KRKGDVEVLD VIYENSLYAK
PCEKAVEAIK NSDLVIIGPS NPITSIGPIL SLNGIKELLK DKKVVVVSPI VGNSAVSGPA
GKLMKAKGYD VSVKGIYEFY KDIVDVLVID NVDKEIAKEI PCEVLITNTI MKTLDDKVRL
AKNIIEFCGS L
