ID   A0A0W1SP62_9EURY        Unreviewed;       330 AA.
AC   A0A0W1SP62;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   19-JAN-2022, entry version 31.
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=AUR66_12425 {ECO:0000313|EMBL:KTG28027.1};
OS   Haloferax profundi.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1544718 {ECO:0000313|EMBL:KTG28027.1, ECO:0000313|Proteomes:UP000053157};
RN   [1] {ECO:0000313|EMBL:KTG28027.1, ECO:0000313|Proteomes:UP000053157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB29 {ECO:0000313|EMBL:KTG28027.1,
RC   ECO:0000313|Proteomes:UP000053157};
RA   Zhang G., Stingl U., Rashid M.;
RT   "Haloferax profundi sp. nov. isolated from the Discovery deep brine-
RT   seawater interface in the Red Sea.";
RL   Submitted (DEC-2015) 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:KTG28027.1}.
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DR   EMBL; LOPV01000145; KTG28027.1; -; Genomic_DNA.
DR   RefSeq; WP_058571838.1; NZ_LOPV01000145.1.
DR   EnsemblBacteria; KTG28027; KTG28027; AUR66_12425.
DR   OrthoDB; 31831at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000053157; 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; 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 {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01257};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01257}.
FT   BINDING         49
FT                   /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01257"
SQ   SEQUENCE   330 AA;  35288 MW;  503B07D33B5AB9AF CRC64;
     MVTFLAGGTG TPKLLDGAGE VFDPAETTVV ANTGDDVELG GHLVCPDVDT VLFWGGGVLD
     TDRWWGIADD TTETDDELHR LADAAGLESG PRFLPDHAQT AGRDIARWRR FSGVAEFMEI
     GDRDRAVHIT RTSLLDEGRS LTDVTRTLAD AFGLAVSLLP MSDDPVATLV HTDEGTMHFQ
     EYWVHHRAEP TVRDVEFRGA DVAEITDDVA AALSDPVVVG PSNPITSIGP MLALEGFREA
     LAETPVVAVS PFVEDRVFSG PAADLMAGVG YDPSTAGVAE AYPFADAFVL DDEDGTDLDR
     PVVRTDTRID GLEDAARVAR AVDEALREVS
//