ID A0A0M8SY02_9ACTN Unreviewed; 319 AA.
AC A0A0M8SY02;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Phosphoenolpyruvate 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=fbiA {ECO:0000256|HAMAP-Rule:MF_01257};
GN ORFNames=ADK55_22100 {ECO:0000313|EMBL:KOU45404.1};
OS Streptomyces sp. WM4235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU45404.1, ECO:0000313|Proteomes:UP000037699};
RN [1] {ECO:0000313|EMBL:KOU45404.1, ECO:0000313|Proteomes:UP000037699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM4235 {ECO:0000313|EMBL:KOU45404.1,
RC ECO:0000313|Proteomes:UP000037699};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of the phosphoenolpyruvate moiety from
CC enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8-
CC hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme
CC F420-0 and GMP. {ECO:0000256|HAMAP-Rule:MF_01257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-didemethyl-8-hydroxy-5-deazariboflavin + enolpyruvoyl-2-
CC diphospho-5'-guanosine = dehydro coenzyme F420-0 + GMP + H(+);
CC Xref=Rhea:RHEA:27510, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:59904, ChEBI:CHEBI:143701, ChEBI:CHEBI:143705;
CC EC=2.7.8.28; 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:KOU45404.1}.
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DR EMBL; LGDE01000338; KOU45404.1; -; Genomic_DNA.
DR RefSeq; WP_053681302.1; NZ_LGDE01000338.1.
DR AlphaFoldDB; A0A0M8SY02; -.
DR PATRIC; fig|1415551.3.peg.4813; -.
DR OrthoDB; 7466225at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000037699; 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:UP000037699};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01257}.
FT BINDING 50
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 319 AA; 32973 MW; B56B413CB02A1F2E CRC64;
MRIVVLAGGI GGARFLRGLK SAVPEAEITV IGNTGDDIHL FGLKVCPDLD TVMYTLGGGI
NEDQGWGRTD ESFTVKEELA AYGVGPTWFG LGDRDFATHI VRTQMIGAGY PLSAVTEALC
DRWQPGVRLL PMSDDRVETH VAITEPGSGE RRVIHFQEYW VKMRAAVDAE AVVPVGAEQA
KPAPGVLEAI AAADVIVFPP SNPVVSVGTI LAVPGIREAV AAASAPVVGL SPIVGGAPVR
GMADKVLAAV GVESTAAAVA LHYGTGLLDG WLVDTADAAA VAEVEAAGIT CRAVPLMMTD
LDATAAMARA ALELAEASR
//
