ID A0A1A2UDI0_MYCSC Unreviewed; 333 AA.
AC A0A1A2UDI0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=A5679_26570 {ECO:0000313|EMBL:OBH86714.1};
OS Mycobacterium scrofulaceum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1783 {ECO:0000313|EMBL:OBH86714.1, ECO:0000313|Proteomes:UP000092207};
RN [1] {ECO:0000313|EMBL:OBH86714.1, ECO:0000313|Proteomes:UP000092207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2838 {ECO:0000313|EMBL:OBH86714.1,
RC ECO:0000313|Proteomes:UP000092207};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBH86714.1}.
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DR EMBL; LZJY01000414; OBH86714.1; -; Genomic_DNA.
DR RefSeq; WP_067310477.1; NZ_LZJY01000414.1.
DR AlphaFoldDB; A0A1A2UDI0; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000092207; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01257}.
FT BINDING 65
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 333 AA; 35301 MW; EB6C7B7212A658ED CRC64;
MKVTVLVGGV GGARFLLGIQ QLLGLGQFAT QQHPDAGTGT HELNAIVNIG DDAWIHGLRV
CPDLDTCMYT LGGGVDPERG WGHRDETWHA KEELARYGVQ PDWFGLGDRD IATHLVRTQM
LNAGYPLSEI TTALCDRWQP GARLLPASDD RCETHVVITD PDDGTRRAIH FQEWWVRYRA
EVPTHSFAFI GAEKATATSE AVAAIADADA ILLAPSNPVV SVGAILAVPG IRAALRSATA
PIVGYSPIIG GKPLRGMADA CLSVIGVEST AEAVGRHYGG RSGTGILDCW LVHEGDHADI
EGVAVTAVPL LMTDPKATAE MVRAGLELAG VTP
//
