ID A0A1N6Y819_9EURY Unreviewed; 336 AA.
AC A0A1N6Y819;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN05421858_1443 {ECO:0000313|EMBL:SIR10631.1};
OS Haladaptatus litoreus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haladaptataceae; Haladaptatus.
OX NCBI_TaxID=553468 {ECO:0000313|EMBL:SIR10631.1, ECO:0000313|Proteomes:UP000186914};
RN [1] {ECO:0000313|Proteomes:UP000186914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7737 {ECO:0000313|Proteomes:UP000186914};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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}.
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DR EMBL; FTNO01000001; SIR10631.1; -; Genomic_DNA.
DR RefSeq; WP_076429216.1; NZ_FTNO01000001.1.
DR AlphaFoldDB; A0A1N6Y819; -.
DR OrthoDB; 59563at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000186914; 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; 2.
DR Gene3D; 3.40.50.10680; CofD-like domains; 2.
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:UP000186914};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01257}.
FT BINDING 49
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 336 AA; 35858 MW; 513E8E954E078B1D CRC64;
MATFLSGGTG TPKLLDGAFS VFSPAETTVV GNTGDDVELG GLLVCPDIDT VLFQQGDVLN
RETWWGIADD TTETHDELHR LAESAGLEGG PRYLPDGQQT AGRKIARWRR FSGVAEFMLL
GDRDRAVHVT RTGLLDEGNS LTETTRILAD AFGSPLDIVP MSDDPVASII HTPEGEMHFQ
EFWVARGGEP EVTDVEFRGA DDASASSAAL SALTDEPVVI GPSNPVTSIG PMLAIDEFRE
ALETATVVAV SPFVEDRVFS GPAGKLMDAV GYEPNTAGVA EAYPFVDAFV LDDEDGTNLD
RPVVRTDTKM DDAADAERVA RAVEQAIEEA KAMEVA
//
