TYRC_ZYMMO
ID TYRC_ZYMMO Reviewed; 293 AA.
AC Q04983; Q5NQG0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cyclohexadienyl dehydrogenase {ECO:0000303|PubMed:7916685};
DE AltName: Full=Arogenate dehydrogenase {ECO:0000303|PubMed:7916685};
DE Short=ADH {ECO:0000303|PubMed:7916685};
DE EC=1.3.1.43 {ECO:0000269|PubMed:7916685};
DE AltName: Full=Prephenate dehydrogenase {ECO:0000303|PubMed:7916685};
DE Short=PDH {ECO:0000303|PubMed:7916685};
DE EC=1.3.1.12 {ECO:0000269|PubMed:7916685};
GN Name=tyrC {ECO:0000303|PubMed:7916685}; OrderedLocusNames=ZMO0420;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=7916685; DOI=10.1111/j.1432-1033.1993.tb17646.x;
RA Zhao G., Xia T., Ingram L.O., Jensen R.A.;
RT "An allosterically insensitive class of cyclohexadienyl dehydrogenase from
RT Zymomonas mobilis.";
RL Eur. J. Biochem. 212:157-165(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: Can function as either prephenate dehydrogenase or as
CC arogenate dehydrogenase in the biosynthesis of L-tyrosine. Catalyzes
CC two analogous reactions: converts prephenate to 4-hydroxyphenylpyruvate
CC and transforms L-arogenate to L-tyrosine. Is not able to utilize
CC NADP(+) instead of NAD(+) as cosubstrate. {ECO:0000269|PubMed:7916685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arogenate + NAD(+) = CO2 + L-tyrosine + NADH;
CC Xref=Rhea:RHEA:12256, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58180, ChEBI:CHEBI:58315; EC=1.3.1.43;
CC Evidence={ECO:0000269|PubMed:7916685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC Evidence={ECO:0000269|PubMed:7916685};
CC -!- ACTIVITY REGULATION: Insensitive to feedback inhibition by L-tyrosine.
CC {ECO:0000269|PubMed:7916685}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for L-arogenate (at pH 6.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:7916685};
CC KM=0.18 mM for prephenate (at pH 6.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:7916685};
CC KM=0.09 mM for NAD(+) (at pH 6.6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:7916685};
CC Note=The KM value obtained for NAD(+) is the same regardless of
CC whether the enzyme is assayed as arogenate dehydrogenase or as
CC prephenate dehydrogenase. Has a greater Vmax with L-arogenate as
CC substrate (about 3-fold higher than with prephenate).
CC {ECO:0000269|PubMed:7916685};
CC pH dependence:
CC Optimum pH is 6.6 for both activities. {ECO:0000269|PubMed:7916685};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000269|PubMed:7916685}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine
CC from L-arogenate (NAD(+) route): step 1/1.
CC {ECO:0000269|PubMed:7916685}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7916685}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {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; M75891; AAA27684.1; -; Genomic_DNA.
DR EMBL; X67208; CAA47647.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89044.1; -; Genomic_DNA.
DR PIR; S29384; S29384.
DR RefSeq; WP_011240335.1; NZ_CP035711.1.
DR AlphaFoldDB; Q04983; -.
DR SMR; Q04983; -.
DR STRING; 264203.ZMO0420; -.
DR PRIDE; Q04983; -.
DR EnsemblBacteria; AAV89044; AAV89044; ZMO0420.
DR GeneID; 58026264; -.
DR KEGG; zmo:ZMO0420; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_0_1_5; -.
DR OMA; MWRDICL; -.
DR OrthoDB; 533829at2; -.
DR UniPathway; UPA00122; UER00959.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0047794; F:cyclohexadienyl dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IGI:UniProtKB.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR Pfam; PF02153; PDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome;
KW Tyrosine biosynthesis.
FT CHAIN 1..293
FT /note="Cyclohexadienyl dehydrogenase"
FT /id="PRO_0000119209"
FT DOMAIN 5..293
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT BINDING 6..30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CONFLICT 42
FT /note="R -> C (in Ref. 1; AAA27684/CAA47647)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="G -> E (in Ref. 1; AAA27684/CAA47647)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="R -> H (in Ref. 1; AAA27684/CAA47647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 32051 MW; 027683380D81146C CRC64;
MTVFKHIAII GLGLIGSSAA RATKAYCPDV TVSLYDKSEF VRDRARALNL GDNVTDDIQD
AVREADLVLL CVPVRAMGIV AAAMAPALKK DVIICDTGSV KVSVIKTLQD NLPNHIIVPS
HPLAGTENNG PDAGFAELFQ DHPVILTPDA HTPAQAIAYI ADYWEEIGGR INLMSAEHHD
HVLALTSHLP HVIAYQLIGM VSGYEKKSRT PIMRYSAGSF RDATRVAASE PRLWQDIMLE
NAPALLPVLD HFIADLKKLR TAIASQDGDY LLEHFKESQK ARLALKTDHD IRP
