ID A0A1I2RNL1_9EURY Unreviewed; 330 AA.
AC A0A1I2RNL1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=SAMN04488063_1990 {ECO:0000313|EMBL:SFG42098.1};
OS Halopelagius inordinatus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=553467 {ECO:0000313|EMBL:SFG42098.1, ECO:0000313|Proteomes:UP000198876};
RN [1] {ECO:0000313|Proteomes:UP000198876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7739 {ECO:0000313|Proteomes:UP000198876};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOOQ01000002; SFG42098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2RNL1; -.
DR STRING; 553467.SAMN04488063_1990; -.
DR OrthoDB; 59563at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000198876; 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 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:UP000198876};
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 330 AA; 35346 MW; 7F828A1C09D25BCE CRC64;
MTTFLAGGTG TPKLLDGAPG VFDPSETTVV ANTGDDVELG GHLVCPDVDT VLFHGGGVLD
TDRWWGIDGD TTETDGELHR LAAAAGVESG PRYLSDEAQT AGRTIARWRR FSGVAEFMEI
GDRDRAVHIT RTSLLDEGRT LTEVTRTLAE AFGLEIDLLP MSDDPVATIV HTDEGEMHFQ
EYWVHRRADP AVEGVEFRGA DEATETEAVL DALSDPVVVG PSNPVTSIGP MLSLPDFEAK
LRETPVVAVS PFVEDEVFSG PAAELMRGVG YEASTAGVAE AYPFADAFVV DDEDGTELDR
PVVRTDTRID GAEDAARVCR AVREALEVVT
//
