ID   FLDI_CLOSG              Reviewed;         264 AA.
AC   Q93AM0;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=(R)-phenyllactate dehydratase activator;
DE            EC=3.6.1.-;
DE   AltName: Full=Initiator of phenyllactate dehydratase {ECO:0000303|PubMed:11967068};
GN   Name=fldI {ECO:0000303|PubMed:11967068};
OS   Clostridium sporogenes.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, SUBUNIT, AND
RP   PATHWAY.
RC   STRAIN=ATCC 3584;
RX   PubMed=11967068; DOI=10.1046/j.1365-2958.2002.02867.x;
RA   Dickert S., Pierik A.J., Buckel W.;
RT   "Molecular characterization of phenyllactate dehydratase and its initiator
RT   from Clostridium sporogenes.";
RL   Mol. Microbiol. 44:49-60(2002).
CC   -!- FUNCTION: Involved in the fermentation of L-phenylalanine via a
CC       Stickland reaction. Required for the activation of the (R)-
CC       phenyllactate dehydratase complex FldABC. Only in the oxidized state,
CC       FldI exhibits significant ATPase activity, which appears to be
CC       essential for unidirectional electron transfer. This protein is
CC       extremely sensitive towards oxygen. {ECO:0000269|PubMed:11967068}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:11967068};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000269|PubMed:11967068};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation.
CC       {ECO:0000305|PubMed:11967068}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11967068}.
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DR   EMBL; AF420489; AAL18809.1; -; Genomic_DNA.
DR   RefSeq; WP_003492348.1; NZ_UAWJ01000006.1.
DR   AlphaFoldDB; Q93AM0; -.
DR   SMR; Q93AM0; -.
DR   GeneID; 45609433; -.
DR   OrthoDB; 1837697at2; -.
DR   BioCyc; MetaCyc:MON-20616; -.
DR   BRENDA; 5.6.1.9; 1517.
DR   UniPathway; UPA00139; -.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR008275; CoA_E_activase.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00241; CoA_E_activ; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Iron; Iron-sulfur; Metal-binding.
FT   CHAIN           1..264
FT                   /note="(R)-phenyllactate dehydratase activator"
FT                   /id="PRO_0000423006"
FT   BINDING         128
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   264 AA;  28076 MW;  A6F77FA2266C6F0B CRC64;
     MADIYTMGVD IGSTASKTVV LKNGKEIVSQ AVISVGAGTS GPKRAIDSVL KDAKLSIEDL
     DYIVSTGYGR NSFDFANKQI SELSCHAKGV YFDNNKARTV IDIGGQDIKV LKLADSGRLL
     NFIMNDKCAA GTGRFLDVMS RVIEVPVDEL GKKALESKNP CTISSTCTVF AESEVISQLA
     RGVKTEDLIA GICKSVASRV ASLAKRSGIE ELVVMSGGVA KNIGVVKAME AELGRDIYIS
     KNSQLNGALG ASLYAYESFQ KERS