FLDB_CLOSG
ID FLDB_CLOSG Reviewed; 407 AA.
AC Q93AL9;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=(R)-phenyllactyl-CoA dehydratase alpha subunit {ECO:0000305|PubMed:10849007, ECO:0000305|PubMed:11967068};
DE EC=4.2.1.175 {ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
DE Flags: Precursor;
GN Name=fldB {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 5-24, 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 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=45490; Method=MALDI; Note=Apparently, about six
CC amino acids are lost during post-translational modification. This
CC result agrees in part with the chemically determined N-terminus, though
CC of bad quality, which starts with the fifth amino acid.;
CC Evidence={ECO:0000269|PubMed:10849007};
CC -!- SIMILARITY: Belongs to the FldB/FldC dehydratase alpha/beta subunit
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF420489; AAL18810.1; -; Genomic_DNA.
DR RefSeq; WP_003492352.1; NZ_UAWJ01000006.1.
DR AlphaFoldDB; Q93AL9; -.
DR SMR; Q93AL9; -.
DR GeneID; 45609432; -.
DR OrthoDB; 437351at2; -.
DR BioCyc; MetaCyc:MON-20597; -.
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 PROPEP 1..4
FT /evidence="ECO:0000269|PubMed:10849007"
FT /id="PRO_0000423003"
FT CHAIN 5..407
FT /note="(R)-phenyllactyl-CoA dehydratase alpha subunit"
FT /id="PRO_0000423004"
SQ SEQUENCE 407 AA; 46238 MW; 8455DFAA6A3F924D CRC64;
MSDRNKEVKE KKAKHYLREI TAKHYKEALE AKERGEKVGW CASNFPQEIA TTLGVKVVYP
ENHAAAVAAR GNGQNMCEHA EAMGFSNDVC GYARVNLAVM DIGHSEDQPI PMPDFVLCCN
NICNQMIKWY EHIAKTLDIP MILIDIPYNT ENTVSQDRIK YIRAQFDDAI KQLEEITGKK
WDENKFEEVM KISQESAKQW LRAASYAKYK PSPFSGFDLF NHMAVAVCAR GTQEAADAFK
MLADEYEENV KTGKSTYRGE EKQRILFEGI ACWPYLRHKL TKLSEYGMNV TATVYAEAFG
VIYENMDELM AAYNKVPNSI SFENALKMRL NAVTSTNTEG AVIHINRSCK LWSGFLYELA
RRLEKETGIP VVSFDGDQAD PRNFSEAQYD TRIQGLNEVM VAKKEAE
