ID A0A2V2MT78_9EURY Unreviewed; 308 AA.
AC A0A2V2MT78;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=2-phospho-L-lactate transferase {ECO:0000256|HAMAP-Rule:MF_01257};
DE EC=2.7.8.28 {ECO:0000256|HAMAP-Rule:MF_01257};
DE AltName: Full=EPPG:FO PEP transferase {ECO:0000256|HAMAP-Rule:MF_01257};
GN Name=cofD {ECO:0000256|HAMAP-Rule:MF_01257};
GN ORFNames=DK846_14610 {ECO:0000313|EMBL:PWR70619.1};
OS Methanospirillum lacunae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=668570 {ECO:0000313|EMBL:PWR70619.1, ECO:0000313|Proteomes:UP000245657};
RN [1] {ECO:0000313|EMBL:PWR70619.1, ECO:0000313|Proteomes:UP000245657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ki8-1 {ECO:0000313|EMBL:PWR70619.1,
RC ECO:0000313|Proteomes:UP000245657};
RA Dueholm M.S., Nielsen P.H., Bakmann L.F., Otzen D.E.;
RT "Draft genome of Methanospirillum lacunae Ki8-1.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01257};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01257};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01257}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01257}.
CC -!- SIMILARITY: Belongs to the CofD family. {ECO:0000256|HAMAP-
CC Rule:MF_01257}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01257}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWR70619.1}.
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DR EMBL; QGMY01000011; PWR70619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2MT78; -.
DR OrthoDB; 59563at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000245657; Unassembled WGS sequence.
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; 1.10.8.240; CofD-like domain; 1.
DR Gene3D; 3.40.50.10680; CofD-like domains; 1.
DR HAMAP; MF_01257; CofD; 1.
DR InterPro; IPR002882; CofD.
DR InterPro; IPR038136; CofD-like_dom_sf.
DR InterPro; IPR010115; FbiA/CofD.
DR NCBIfam; TIGR01819; F420_cofD; 1.
DR PANTHER; PTHR43007; 2-PHOSPHO-L-LACTATE TRANSFERASE; 1.
DR PANTHER; PTHR43007:SF1; 2-PHOSPHO-L-LACTATE TRANSFERASE; 1.
DR Pfam; PF01933; CofD; 1.
DR SUPFAM; SSF142338; CofD-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01257};
KW Reference proteome {ECO:0000313|Proteomes:UP000245657};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01257}.
FT BINDING 58
FT /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT /ligand_id="ChEBI:CHEBI:59904"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01257"
SQ SEQUENCE 308 AA; 33739 MW; 6810121EBF64E1CB CRC64;
MSLSWEDTIT VTFLSGGTGT PKLLQGARLA LNDKDIAVIV NTAEDLWYQG GHISPDIDTV
MYLFAGILNT KTWWGIDGDT FVTHEQFRSI GVDTYLAVGD KDRAVELLRG ELLKEGMTLS
QATCDLSSRL SVHATIIPMT DQEYTTMIET KDGIIHFQEY WVKHRGSVEI SKVLRVPERR
PDASTGALEA MKKSDLIIIG PSNPITSISP ILECNGIIDL LKQKPVVAVS PFIGDKPVSG
PARDLMVARG FEPTSAGVYA AYAEFVDLFV QDIRDPVDVP GAIRCDTLMT SPDISKGIID
LILDRMPV
//
