FLDC_CLOSG
ID FLDC_CLOSG Reviewed; 374 AA.
AC Q93AL8;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=(R)-phenyllactyl-CoA dehydratase beta subunit {ECO:0000305|PubMed:10849007, ECO:0000305|PubMed:11967068};
DE EC=4.2.1.175 {ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
GN Name=fldC {ECO:0000303|PubMed:10849007, 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, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND COFACTOR.
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).
RN [2]
RP PROTEIN SEQUENCE OF 2-29, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MASS
RP SPECTROMETRY, SUBUNIT, AND PATHWAY.
RC STRAIN=ATCC 3584;
RX PubMed=10849007; DOI=10.1046/j.1432-1327.2000.01427.x;
RA Dickert S., Pierik A.J., Linder D., Buckel W.;
RT "The involvement of coenzyme A esters in the dehydration of (R)-
RT phenyllactate to (E)-cinnamate by Clostridium sporogenes.";
RL Eur. J. Biochem. 267:3874-3884(2000).
CC -!- FUNCTION: Component of the phenyllactate dehydratase complex FldABC
CC that is involved in the fermentation of L-phenylalanine via a Stickland
CC reaction. This complex catalyzes the reversible syn-dehydration of (R)-
CC phenyllactate to (E)-cinnamate in two steps, a CoA-transfer from
CC cinnamoyl-CoA to phenyllactate, catalyzed by FldA, followed by the
CC dehydration of phenyllactyl-CoA to cinnamoyl-CoA, catalyzed by FldB and
CC FldC. Requires the activator FldI to initiate catalysis.
CC {ECO:0000269|PubMed:10849007, ECO:0000269|PubMed:11967068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-phenyllactoyl-CoA = (E)-cinnamoyl-CoA + H2O;
CC Xref=Rhea:RHEA:38355, ChEBI:CHEBI:15377, ChEBI:CHEBI:57252,
CC ChEBI:CHEBI:57254; EC=4.2.1.175;
CC Evidence={ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-(4-hydroxyphenyl)lactoyl-CoA = (E)-4-coumaroyl-CoA +
CC H2O; Xref=Rhea:RHEA:60108, ChEBI:CHEBI:15377, ChEBI:CHEBI:85008,
CC ChEBI:CHEBI:143007; EC=4.2.1.175;
CC Evidence={ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-(indol-3-yl)lactoyl-CoA = (E)-3-(indol-3-yl)acryloyl-CoA
CC + H2O; Xref=Rhea:RHEA:60112, ChEBI:CHEBI:15377, ChEBI:CHEBI:143008,
CC ChEBI:CHEBI:143009; EC=4.2.1.175;
CC Evidence={ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
CC Note=Appears to contain about 1 [4Fe-4S] cluster per heterodimer FldBC.
CC {ECO:0000269|PubMed:10849007};
CC -!- COFACTOR:
CC Note=No flavin coud be detected in the FldABC complex, and the addition
CC of FAD, FMN or riboflavin to the dehydratase do not increase enzymatic
CC activity. {ECO:0000269|PubMed:11967068};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for (E)-cinnamoyl-CoA (at pH 8 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:11967068};
CC Note=kcat is 1 sec(-1) (at pH 8 and 20 degrees Celsius). Values have
CC been measured with the FldABC complex. {ECO:0000269|PubMed:11967068};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation.
CC {ECO:0000305|PubMed:10849007}.
CC -!- SUBUNIT: Part of the heterotrimeric phenyllactate dehydratase complex
CC FldABC, composed of (R)-phenyllactate CoA-transferase (FldA) and a
CC heterodimeric (R)-phenyllactyl-CoA dehydratase (FldB and FldC).
CC {ECO:0000269|PubMed:10849007, ECO:0000269|PubMed:11967068}.
CC -!- MASS SPECTROMETRY: Mass=37340; Method=MALDI; Note=It seems that about
CC 50 C-terminal amino acids have been lost by post-translational
CC modification.; Evidence={ECO:0000269|PubMed:10849007};
CC -!- SIMILARITY: Belongs to the FldB/FldC dehydratase alpha/beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AF420489; AAL18811.1; -; Genomic_DNA.
DR RefSeq; WP_003492354.1; NZ_UAWJ01000006.1.
DR AlphaFoldDB; Q93AL8; -.
DR SMR; Q93AL8; -.
DR PRIDE; Q93AL8; -.
DR GeneID; 45609431; -.
DR OrthoDB; 1815612at2; -.
DR BioCyc; MetaCyc:MON-20596; -.
DR BRENDA; 4.2.1.175; 1517.
DR UniPathway; UPA00139; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
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; IPR010327; FldB/FldC_alpha/beta.
DR Pfam; PF06050; HGD-D; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10849007"
FT CHAIN 2..374
FT /note="(R)-phenyllactyl-CoA dehydratase beta subunit"
FT /id="PRO_0000423005"
SQ SEQUENCE 374 AA; 43149 MW; 84297814477B60B0 CRC64;
MSNSDKFFND FKDIVENPKK YIMKHMEQTG QKAIGCMPLY TPEELVLAAG MFPVGVWGSN
TELSKAKTYF PAFICSILQT TLENALNGEY DMLSGMMITN YCDSLKCMGQ NFKLTVENIE
FIPVTVPQNR KMEAGKEFLK SQYKMNIEQL EKISGNKITD ESLEKAIEIY DEHRKVMNDF
SMLASKYPGI ITPTKRNYVM KSAYYMDKKE HTEKVRQLMD EIKAIEPKPF EGKRVITTGI
IADSEDLLKI LEENNIAIVG DDIAHESRQY RTLTPEANTP MDRLAEQFAN RECSTLYDPE
KKRGQYIVEM AKERKADGII FFMTKFCDPE EYDYPQMKKD FEEAGIPHVL IETDMQMKNY
EQARTAIQAF SETL
