ID Q96Y98_SULTO Unreviewed; 341 AA.
AC Q96Y98;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE SubName: Full=Chorismate mutase/prephenate dehydrogenase {ECO:0000313|EMBL:BAB67379.1};
DE EC=1.3.1.12 {ECO:0000313|EMBL:BAB67379.1};
DE EC=5.4.99.5 {ECO:0000313|EMBL:BAB67379.1};
GN Name=tyrA {ECO:0000313|EMBL:BAB67379.1};
GN Synonyms=ST2270 {ECO:0000313|EMBL:BAB67379.1};
GN OrderedLocusNames=STK_22700 {ECO:0000313|EMBL:BAB67379.1};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063 {ECO:0000313|EMBL:BAB67379.1, ECO:0000313|Proteomes:UP000001015};
RN [1] {ECO:0000313|Proteomes:UP000001015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7
RC {ECO:0000313|Proteomes:UP000001015};
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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DR EMBL; BA000023; BAB67379.1; -; Genomic_DNA.
DR RefSeq; WP_010980354.1; NC_003106.2.
DR AlphaFoldDB; Q96Y98; -.
DR STRING; 273063.STK_22700; -.
DR GeneID; 1460352; -.
DR KEGG; sto:STK_22700; -.
DR PATRIC; fig|273063.9.peg.2574; -.
DR eggNOG; arCOG00245; Archaea.
DR OMA; MAYIQVA; -.
DR OrthoDB; 34329at2157; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.59.10; Chorismate mutase; 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; IPR008244; Chor_mut/prephenate_DH_T.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR010950; Chorismate_mutase_arc.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR003099; Prephen_DH.
DR NCBIfam; TIGR01791; CM_archaeal; 1.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR PIRSF; PIRSF001499; Chor_mut_pdh_Tpr; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:BAB67379.1};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAB67379.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001015}.
FT DOMAIN 1..90
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 93..341
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 341 AA; 39052 MW; 8814AD1FA198D38D CRC64;
MSAEIDELRK EIEAIDKQIL ELLSRRLKIS AKIGEIKSRI GKDVTDEKRE QKVREYWYNY
ARNLGIPDSM VESILPILFS YSKMVQINPG KKKNITVIGY GGMARSLISL FSLVGHNVVV
TGRNKEKAER LASEFKVVYM DLDSALNWGE YIILALSPSS FDYILRISPK FTSKVVMDIF
SSKNEIFKEL EKLSEIYSFN YISTHPLFGP ITYPVGERIV IIPSKTSKNV NEIVNFWREC
GLNTTVSTVE EHEKAMAIVQ VLAHFYILGL HRSIDELRKE LGIENLSNFY TTNFKELNKI
IEKVSNILPV ILEIQKSNPY AYKVRDIGVN ELQKIKEELG G
//