TYRA_BACSU
ID TYRA_BACSU Reviewed; 371 AA.
AC P20692;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Prephenate dehydrogenase;
DE Short=PDH;
DE EC=1.3.1.12;
GN Name=tyrA; OrderedLocusNames=BSU22610;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3106153; DOI=10.1016/0378-1119(86)90394-x;
RA Henner D.J., Band L., Flaggs G., Chen E.;
RT "The organization and nucleotide sequence of the Bacillus subtilis hisH,
RT tyrA and aroE genes.";
RL Gene 49:147-152(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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 -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M80245; AAA20868.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14177.1; -; Genomic_DNA.
DR RefSeq; NP_390142.1; NC_000964.3.
DR RefSeq; WP_003230615.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P20692; -.
DR SMR; P20692; -.
DR STRING; 224308.BSU22610; -.
DR PaxDb; P20692; -.
DR PRIDE; P20692; -.
DR EnsemblBacteria; CAB14177; CAB14177; BSU_22610.
DR GeneID; 939013; -.
DR KEGG; bsu:BSU22610; -.
DR eggNOG; COG0287; Bacteria.
DR InParanoid; P20692; -.
DR OMA; MWRDICL; -.
DR PhylomeDB; P20692; -.
DR BioCyc; BSUB:BSU22610-MON; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IBA:GO_Central.
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; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF02153; PDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW Oxidoreductase; Reference proteome; Tyrosine biosynthesis.
FT CHAIN 1..371
FT /note="Prephenate dehydrogenase"
FT /id="PRO_0000119192"
FT DOMAIN 6..295
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT DOMAIN 300..371
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 7..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 371 AA; 41434 MW; 9254360B94526C00 CRC64;
MNQMKDTILL AGLGLIGGSI ALAIKKNHPG KRIIGIDISD EQAVAALKLG VIDDRADSFI
SGVKEAATVI IATPVEQTLV MLEELAHSGI EHELLITDVG STKQKVVDYA DQVLPSRYQF
VGGHPMAGSH KSGVAAAKEF LFENAFYILT PGQKTDKQAV EQLKNLLKGT NAHFVEMSPE
EHDGVTSVIS HFPHIVAASL VHQTHHSENL YPLVKRFAAG GFRDITRIAS SSPAMWRDIL
LHNKDKILDR FDEWIREIDK IRTYVEQEDA ENLFRYFKTA KDYRDGLPLR QKGAIPAFYD
LYVDVPDHPG VISEITAILA AERISITNIR IIETREDING ILRISFQSDD DRKRAEQCIE
ARAEYETFYA D
