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2-phospho-L-lactate transferase (EC 2.7.8.28) (LPPG:FO 2-phospho-L-lactate transferase)

 COFD_METJA              Reviewed;         311 AA.
Q58653;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 94.
RecName: Full=2-phospho-L-lactate transferase;
EC=2.7.8.28;
AltName: Full=LPPG:FO 2-phospho-L-lactate transferase;
Name=cofD; OrderedLocusNames=MJ1256;
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
Archaea; Euryarchaeota; Methanococci; Methanococcales;
Methanocaldococcaceae; Methanocaldococcus.
NCBI_TaxID=243232;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087; DOI=10.1126/science.273.5278.1058;
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus
jannaschii.";
Science 273:1058-1073(1996).
[2]
FUNCTION, CHARACTERIZATION, SUBUNIT, AND MUTAGENESIS OF SER-211.
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=11888293; DOI=10.1021/bi011937v;
Graupner M., Xu H., White R.H.;
"Characterization of the 2-phospho-L-lactate transferase enzyme
involved in coenzyme F(420) biosynthesis in Methanococcus
jannaschii.";
Biochemistry 41:3754-3761(2002).
-!- FUNCTION: Catalyzes the transfer of the 2-phospholactate moiety
from lactyl (2) diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-
8-hydroxy-5-deazariboflavin (FO) with the formation of the L-
lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-
deazariboflavin (F420-0) and GMP. To a lesser extent CofD also
catalyzes a number of additional reactions that include the
formation of FO-P, when the enzyme is incubated with FO and GDP,
GTP, pyrophosphate, or tripolyphosphate and the hydrolysis of
F420-0 to FO. {ECO:0000269|PubMed:11888293}.
-!- CATALYTIC ACTIVITY: (2S)-lactyl-2-diphospho-5'-guanosine + 7,8-
didemethyl-8-hydroxy-5-deazariboflavin = guanosine 5'-phosphate +
coenzyme F420-0.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Inhibited by EDTA.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=32 uM for FO;
KM=17 uM for LPPG;
KM=515 uM for LPPA;
Vmax=1.4 umol/min/mg enzyme with LPPG as substrate;
Vmax=0.1 umol/min/mg enzyme with LPPA as substrate;
Temperature dependence:
Optimum temperature is about 37 degrees Celsius. Thermostable.
Still fully active after heating at 80 degrees Celsius for 24
hours. Activity begins to decrease after heating at 98 degrees
Celsius for 30 minutes. Inactive after heating at 110 degrees
Celsius for 30 minutes.;
-!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11888293}.
-!- SIMILARITY: Belongs to the CofD family. {ECO:0000305}.
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EMBL; L77117; AAB99260.1; -; Genomic_DNA.
PIR; G64456; G64456.
RefSeq; WP_010870769.1; NC_000909.1.
ProteinModelPortal; Q58653; -.
SMR; Q58653; -.
STRING; 243232.MJ_1256; -.
EnsemblBacteria; AAB99260; AAB99260; MJ_1256.
GeneID; 1452154; -.
KEGG; mja:MJ_1256; -.
eggNOG; arCOG04395; Archaea.
eggNOG; COG0391; LUCA.
InParanoid; Q58653; -.
KO; K11212; -.
OMA; DLDTVMY; -.
OrthoDB; POG093Z0AHL; -.
PhylomeDB; Q58653; -.
BioCyc; MetaCyc:MONOMER-12181; -.
BioCyc; MJAN243232:G1GKE-1363-MONOMER; -.
BRENDA; 2.7.8.28; 3260.
SABIO-RK; Q58653; -.
UniPathway; UPA00071; -.
Proteomes; UP000000805; Chromosome.
GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IDA:MENGO.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
GO; GO:0009108; P:coenzyme biosynthetic process; IBA:GO_Central.
CDD; cd07186; CofD_like; 1.
HAMAP; MF_01257; CofD; 1.
InterPro; IPR002882; CofD/UPF0052.
InterPro; IPR010115; P-lactate_Trfase.
PANTHER; PTHR43007; PTHR43007; 1.
Pfam; PF01933; UPF0052; 1.
TIGRFAMs; TIGR01819; F420_cofD; 1.
1: Evidence at protein level;
Complete proteome; Magnesium; Reference proteome; Transferase.
CHAIN 1 311 2-phospho-L-lactate transferase.
/FTId=PRO_0000145772.
MUTAGEN 211 211 S->A: No change in activity.
{ECO:0000269|PubMed:11888293}.
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


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