TYRA_MYCTU
ID TYRA_MYCTU Reviewed; 323 AA.
AC O69721; I6Y4F9; L0TGF7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 4.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000303|PubMed:16889979};
DE Short=PDH {ECO:0000303|PubMed:16889979};
DE EC=1.3.1.12 {ECO:0000269|PubMed:16889979};
GN Name=tyrA {ECO:0000303|PubMed:16889979};
GN OrderedLocusNames=Rv3754 {ECO:0000312|EMBL:CCP46581.1},
GN RVBD_3754 {ECO:0000312|EMBL:AFN51778.1};
GN ORFNames=P425_03907 {ECO:0000312|EMBL:KBJ24829.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 4-24, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=H37Rv;
RX PubMed=16889979; DOI=10.1016/j.pep.2006.05.020;
RA Xu S., Yang Y., Jin R., Zhang M., Wang H.;
RT "Purification and characterization of a functionally active Mycobacterium
RT tuberculosis prephenate dehydrogenase.";
RL Protein Expr. Purif. 49:151-158(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent conversion of prephenate to p-
CC hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key
CC regulatory enzyme in tyrosine biosynthesis. Displays no chorismate
CC mutase (CM) activity, in contrast to TyrA from E.coli and some other
CC bacteria, that are bifunctional and possess a CM domain.
CC {ECO:0000269|PubMed:16889979}.
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:16889979};
CC -!- ACTIVITY REGULATION: Is inhibited by NaCl; more than half of the enzyme
CC activity is abolished in the presence of 10 uM of NaCl.
CC {ECO:0000269|PubMed:16889979}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for prephenate (at pH 7.9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16889979};
CC KM=0.28 mM for NAD(+) (at pH 7.9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16889979};
CC Note=kcat is 170.36 sec(-1) toward prephenate, and 356.07 sec(-1)
CC toward NAD(+) (at pH 7.9 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:16889979};
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:16889979};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Is not stable even stored
CC at -80 degrees Celsius. About 50% of the activity is lost when stored
CC at 4 degrees Celsius for 24 hours. {ECO:0000269|PubMed:16889979};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000305|PubMed:16889979}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFN51778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
CC Sequence=CCP46581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
CC Sequence=KBJ24829.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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; AL123456; CCP46581.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP003248; AFN51778.1; ALT_INIT; Genomic_DNA.
DR EMBL; JLDD01000048; KBJ24829.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_218271.3; NC_000962.3.
DR RefSeq; WP_003899677.1; NZ_NVQJ01000009.1.
DR AlphaFoldDB; O69721; -.
DR SMR; O69721; -.
DR STRING; 83332.Rv3754; -.
DR BindingDB; O69721; -.
DR PaxDb; O69721; -.
DR PRIDE; O69721; -.
DR GeneID; 45427754; -.
DR GeneID; 885559; -.
DR KEGG; mtu:Rv3754; -.
DR KEGG; mtv:RVBD_3754; -.
DR PATRIC; fig|83332.111.peg.4176; -.
DR TubercuList; Rv3754; -.
DR eggNOG; COG0287; Bacteria.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000001584; Chromosome.
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:0006571; P:tyrosine biosynthetic process; IBA:GO_Central.
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..323
FT /note="Prephenate dehydrogenase"
FT /id="PRO_0000432509"
FT DOMAIN 8..291
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
SQ SEQUENCE 323 AA; 33099 MW; 5B110E468DAF0696 CRC64;
MTRTVAAPPV CVLGLGLIGG SIMRAAAAAG REVFGYNRSV EGAHGARSDG FDAITDLNQT
LTRAAATEAL IVLAVPMPAL PGMLAHIRKS APGCPLTDVT SVKCAVLDEV TAAGLQARYV
GGHPMTGTAH SGWTAGHGGL FNRAPWVVSV DDHVDPTVWS MVMTLALDCG AMVVPAKSDE
HDAAAAAVSH LPHLLAEALA VTAAEVPLAF ALAAGSFRDA TRVAATAPDL VRAMCEANTG
QLAPAADRII DLLSRARDSL QSHGSIADLA DAGHAARTRY DSFPRSDIVT VVIGADKWRE
QLAAAGRAGG VITSALPSLD SPQ
