ID A0A0U3PUE4_9ACTN Unreviewed; 319 AA.
AC A0A0U3PUE4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=AS200_27270 {ECO:0000313|EMBL:ALV35333.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV35333.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV35333.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV35333.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-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}.
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DR EMBL; CP013743; ALV35333.1; -; Genomic_DNA.
DR RefSeq; WP_058924949.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PUE4; -.
DR STRING; 1725411.AS200_27270; -.
DR KEGG; scx:AS200_27270; -.
DR OrthoDB; 7466225at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000068029; Chromosome.
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:UP000068029};
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; 33657 MW; BC29EB4EA0AAAD65 CRC64;
MRIVVLAGGI GGARFLRGLK KAAPDADITV IGNTGDDIHL FGLKVCPDLD TVMYTLGGGI
NEEQGWGRAD ETFHLKEELG AYGVGPEWFG LGDRDFATHI VRTQMIGAGY PLSAVTQALC
DRWQPGVRLI PMTDDRVETH VAVEIDGERK AVHFQEYWVR LRASVPAEAV VPVGAEQAKP
APGVLEAIAE ADVVLFPPSN PVVSVGTILA VPGIREAIAE AGVPVVGLSP IVGDAPVRGM
ADKVLAAVGV ESSAAAVAEH YGSGLLDGWL VDTRDADAVE RVEAAGIRCR AVPLMMTDLD
ATARMAREAL ELAEEVRAS
//
