FLDH_CLOS3
ID FLDH_CLOS3 Reviewed; 331 AA.
AC G9EZR6;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Aromatic 2-oxoacid reductase {ECO:0000305};
DE EC=1.1.1.110 {ECO:0000250|UniProtKB:J7SHB8, ECO:0000269|PubMed:10849007};
DE AltName: Full=Phenyllactate dehydrogenase {ECO:0000303|PubMed:10849007};
GN Name=fldH {ECO:0000303|PubMed:10849007}; ORFNames=IYC_08803;
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 1-29, FUNCTION IN PHENYLALANINE FERMENTATION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 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: Essential for the reductive metabolism of L-phenylalanine, L-
CC tyrosine and L-tryptophan (By similarity). Catalyzes the conversion of
CC phenylpyruvic acid to phenyllactic acid, 4-hydroxy-phenylpyruvic acid
CC to 4-hydroxy-phenyllactic acid, and indolepyruvic acid to indolelactic
CC acid (PubMed:10849007) (By similarity). {ECO:0000250|UniProtKB:J7SHB8,
CC ECO:0000269|PubMed:10849007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-phenyllactate + NAD(+) = 3-phenylpyruvate + H(+) + NADH;
CC Xref=Rhea:RHEA:38351, ChEBI:CHEBI:11009, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.110; Evidence={ECO:0000269|PubMed:10849007};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38353;
CC Evidence={ECO:0000269|PubMed:10849007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-
CC hydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:10780,
CC ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.110;
CC Evidence={ECO:0000250|UniProtKB:J7SHB8};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10782;
CC Evidence={ECO:0000250|UniProtKB:J7SHB8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(indol-3-yl)lactate + NAD(+) = H(+) + indole-3-pyruvate +
CC NADH; Xref=Rhea:RHEA:20133, ChEBI:CHEBI:15378, ChEBI:CHEBI:17282,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.110; Evidence={ECO:0000250|UniProtKB:J7SHB8};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20135;
CC Evidence={ECO:0000250|UniProtKB:J7SHB8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for phenylpyruvate {ECO:0000269|PubMed:10849007};
CC KM=10 uM for NADH {ECO:0000269|PubMed:10849007};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:10849007};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:10849007}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; JH470519; EHN15453.1; -; Genomic_DNA.
DR RefSeq; WP_003492363.1; NZ_JH470519.1.
DR AlphaFoldDB; G9EZR6; -.
DR SMR; G9EZR6; -.
DR GeneID; 45609426; -.
DR HOGENOM; CLU_019796_1_1_9; -.
DR BioCyc; MetaCyc:MON-8131; -.
DR SABIO-RK; G9EZR6; -.
DR Proteomes; UP000005747; Unassembled WGS sequence.
DR GO; GO:0047995; F:hydroxyphenylpyruvate reductase activity; IEA:RHEA.
DR GO; GO:0047722; F:indolelactate dehydrogenase (NADH) activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0097256; F:phenyllactate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IDA:UniProtKB.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Phenylalanine catabolism;
KW Tryptophan catabolism; Tyrosine catabolism.
FT CHAIN 1..331
FT /note="Aromatic 2-oxoacid reductase"
FT /id="PRO_0000423007"
FT ACT_SITE 234
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 263
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 295
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 154..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 205..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 232..234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
SQ SEQUENCE 331 AA; 36507 MW; F18B3E10244562FB CRC64;
MKILAYCVRP DEIDSFKNFS EKYGHTVDLI PDSFGPSVAH LAKGYDGISI LGNDTCNREA
LEKIKDCGIK YLATRTAGVN NIDFDAAKEF GINVANVPAY SPNSVSEFTV GLALSLTRKI
PFALKRVELN NFALGGLIGV ELRNLTLGVI GTGRIGLKVI EGFSGFGMKK MIGYDIFENE
KAKEYIEYKS LDEVYKEADI ITLHAPLTDD NYHMIGKESI AKMKDGVFII NAARGALIDS
EALIEGLKSG KIAGAALDSY EYEQGVFHNN KMNEIMKDDT LARLKSFPNV VITPHLGFYT
DEAVSNMVEI TLMNLQEFEL KGTCKNQRVC K
