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   27-MAR-2024, entry version 146.
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; Pseudomonadota; 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   KEGG; zmo:ZMO0420; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_0_1_5; -.
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   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//