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Database: UniProt
Entry: G9EZR6
LinkDB: G9EZR6
Original site: G9EZR6 
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   16-JAN-2019, entry version 30.
DE   RecName: Full=Phenyllactate dehydrogenase {ECO:0000303|PubMed:10849007};
DE            EC=1.1.1.- {ECO:0000269|PubMed:10849007};
GN   Name=fldH {ECO:0000303|PubMed:10849007}; ORFNames=IYC_08803;
OS   Clostridium sporogenes (strain ATCC 7955 / DSM 767 / NBRC 16411 /
OS   NCIMB 8053 / NCTC 8594 / PA 3679).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; 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
RC   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, CATALYTIC ACTIVITY,
RP   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: Involved in the fermentation of L-phenylalanine via a
CC       Stickland reaction. Catalyzes the reduction of phenylpyruvate to
CC       yield (R)-phenyllactate. {ECO:0000269|PubMed:10849007}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-3-phenyllactate + NAD(+) = 3-phenylpyruvate + H(+) +
CC         NADH; Xref=Rhea:RHEA:38351, ChEBI:CHEBI:11009,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18005, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:10849007};
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; L-phenylalanine degradation.
CC       {ECO:0000305|PubMed:10849007}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; JH470519; EHN15453.1; -; Genomic_DNA.
DR   RefSeq; WP_003492363.1; NZ_JH470519.1.
DR   SMR; G9EZR6; -.
DR   PRIDE; G9EZR6; -.
DR   EnsemblBacteria; EHN15453; EHN15453; IYC_08803.
DR   BioCyc; MetaCyc:MONOMER-8131; -.
DR   SABIO-RK; G9EZR6; -.
DR   UniPathway; UPA00139; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0097256; F:phenyllactate dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IDA:UniProtKB.
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.
FT   CHAIN         1    331       Phenyllactate dehydrogenase.
FT                                /FTId=PRO_0000423007.
FT   NP_BIND     154    155       NAD. {ECO:0000250}.
FT   NP_BIND     232    234       NAD. {ECO:0000250}.
FT   NP_BIND     295    298       NAD. {ECO:0000250}.
FT   ACT_SITE    234    234       {ECO:0000250}.
FT   ACT_SITE    263    263       {ECO:0000250}.
FT   ACT_SITE    295    295       Proton donor. {ECO:0000250}.
FT   BINDING     258    258       NAD. {ECO:0000250}.
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
//
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