FLDZ_CLOS3
ID FLDZ_CLOS3 Reviewed; 665 AA.
AC G9F1Y9;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Cinnamate reductase {ECO:0000303|PubMed:10849007};
DE EC=1.3.1.- {ECO:0000269|PubMed:10849007};
GN Name=fldZ {ECO:0000303|PubMed:10849007}; ORFNames=IYC_12859;
OS Clostridium sporogenes (strain ATCC 7955 / DSM 767 / NBRC 16411 / NCIMB
OS 8053 / NCTC 8594 / PA 3679).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1075091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7955 / DSM 767 / NBRC 16411 / NCIMB 8053 / NCTC 8594 / PA 3679;
RA Bradbury M., Greenfield P., Midgley D., Li D., Tran-Dinh N., Brown J.;
RT "Whole genome shotgun sequencing of Clostridium 'sporogenes'.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, 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: Involved in the fermentation of L-phenylalanine via a
CC Stickland reaction. Catalyzes the reduction of (E)-cinnamate to yield
CC 3-phenylpropionate. {ECO:0000269|PubMed:10849007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpropanoate + NAD(+) = (E)-cinnamate + H(+) + NADH;
CC Xref=Rhea:RHEA:50944, ChEBI:CHEBI:15378, ChEBI:CHEBI:15669,
CC ChEBI:CHEBI:51057, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:10849007};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P42593};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation.
CC {ECO:0000305|PubMed:10849007}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000305}.
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DR EMBL; JH470528; EHN14667.1; -; Genomic_DNA.
DR RefSeq; WP_003493847.1; NZ_JH470528.1.
DR AlphaFoldDB; G9F1Y9; -.
DR SMR; G9F1Y9; -.
DR HOGENOM; CLU_012153_1_1_9; -.
DR UniPathway; UPA00139; -.
DR Proteomes; UP000005747; Unassembled WGS sequence.
DR GO; GO:0047540; F:2-enoate reductase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; IMP:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; FMN; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..665
FT /note="Cinnamate reductase"
FT /id="PRO_0000423008"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 109
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 230
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 319
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 341..342
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 365
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 368
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 372
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 384
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 434
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 442
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 452
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 479
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
SQ SEQUENCE 665 AA; 73002 MW; 8573471F510B4361 CRC64;
MKDQYKVLYD PIKIGKLEIK NRYVLAPMGP GGMCNADGSF NKRGIEFYVE RAKGGTGLIM
TGVTMVENNI EKCALPSMPC PTINPLNFIT TGNEMTERVH AYGAKIFLQL SAGFGRVSIP
SIVGKVAVAP SKIPHRFLPG VTCRELTTEE VKEYVKAFGE SAEIAKKAGF DGVEIHAVHE
GYLLDQFAIS FFNHRTDEYG GSLENRLRFA CEVVQEIKKR CGQDFPVSLR YSIKSFIKDW
CKGGLPDEEF EEKGRDIPEG IEAAKILVAA GYDALNGDVG SYDSWYWSHP PMYQKKGLYL
PYNEILKKVV DVPIITAGRM EDPELSSDAI LSGKTDMIAL GRPLLADAEI PNKIFEDKYD
KVRPCLSCQE GCMGRLQNFA TVSCAVNPAC GREKEYGLKK AEQIKKVLIV GGGVAGMEAA
RVAAIRGHKV TLIEKNGYLG GNIVPGGVPD FKDDDRALVK WYEGILKDLG VEIKLNVAAS
KENIKEFGAD EVLLATGSSP RTLTIEGADK VYSAEDVLME RKNVGEKVII IGGGLVGCET
ALWLKQQGKE VTIVEMQNDI LQVGGPLCHA NHDMLIDLIK FNKIDVKASS YISKKTDEGF
VLNTNGEESI INADSAVVAI GYLSEKDLYS EVRFDIPNAR LIGDANKVQN IMYAIWSAYE
VAKNI
