ID A0A1Z2L683_9ACTN Unreviewed; 322 AA.
AC A0A1Z2L683;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=cofD {ECO:0000313|EMBL:ARZ69800.1};
GN Synonyms=fbiA {ECO:0000256|HAMAP-Rule:MF_01257};
GN ORFNames=SMD11_4189 {ECO:0000313|EMBL:ARZ69800.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ69800.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ69800.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ69800.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-2017) 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; CP021744; ARZ69800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2L683; -.
DR KEGG; salj:SMD11_4189; -.
DR OrthoDB; 7466225at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000195755; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01257}.
FT BINDING 51
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 322 AA; 33435 MW; 5CA29B5A1158D8EC CRC64;
MQRIVVLAGG IGGARFLRGL KSAAPDADIT VIGNTGDDIH LFGLKVCPDL DTVMYTLGGG
IHEEQGWGRA GETFAVKEEL AAYGVGPAWF GLGDRDFATH IVRTQMLAAG YPLSAVTEAL
CERWRPGVRL IPMSDDRVET HVMTDDPEAA GGRKAIHFQE YWVRLRAEVP AHAIVPVGAD
EAKPAPGVLE ALAEADVILF PPSNPVVSVG TILSVPGVRE AVAASAAPVV GLSPIVGDAP
VRGMADKVLA AVGVESTAAA VARHYGSGLI DGWLVDTVDA GAVPDVEAAG IRCRAVPLMM
TDVEATARMA AEALALAAEV RA
//
