COFD_METHJ
ID COFD_METHJ Reviewed; 297 AA.
AC Q2FRU9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Mhun_2444;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD42145.1; -; Genomic_DNA.
DR RefSeq; WP_011449403.1; NC_007796.1.
DR AlphaFoldDB; Q2FRU9; -.
DR SMR; Q2FRU9; -.
DR STRING; 323259.Mhun_2444; -.
DR EnsemblBacteria; ABD42145; ABD42145; Mhun_2444.
DR GeneID; 3922432; -.
DR KEGG; mhu:Mhun_2444; -.
DR eggNOG; arCOG04395; Archaea.
DR HOGENOM; CLU_055795_1_0_2; -.
DR OMA; DLDTVMY; -.
DR OrthoDB; 31831at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001941; 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..297
FT /note="2-phospho-L-lactate transferase"
FT /id="PRO_1000165108"
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 297 AA; 32662 MW; 6DC79338119E1F3C CRC64;
MITFLSGGTG TPKLLEGARN MLPDSDISVI VNTGEDIWYQ GGHISPDVDT VMYLFAGLLN
TDTWWGVRGD SFLTHDVLKT LLPASYMSIG DKDRAVHIAR AEWLKKGMTL TRVTQQLCSH
FGVSTTILPM SDSPYTTYVR TAKGDIHFQE YWVRYRGNTD ICAVLHVPDE QPPATPEVID
AIRKAEVVII GPSNPVTSIL PILSCTGVRE ELAQKKVIAI SPFIGEGPVS GPAAQLMKTM
KYPADSTGVR ALYADLVDVF IQDERDTAQV PGSVRLDTLM KTPAIAERLM REILTRL