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Database: UniProt
Entry: K9XMV5_STAC7
LinkDB: K9XMV5_STAC7
Original site: K9XMV5_STAC7 
ID   K9XMV5_STAC7            Unreviewed;       396 AA.
AC   K9XMV5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:AFZ33843.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:AFZ33843.1};
GN   OrderedLocusNames=Sta7437_0226 {ECO:0000313|EMBL:AFZ33843.1};
OS   Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC   Stanieria.
OX   NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ33843.1, ECO:0000313|Proteomes:UP000010473};
RN   [1] {ECO:0000313|Proteomes:UP000010473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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DR   EMBL; CP003653; AFZ33843.1; -; Genomic_DNA.
DR   RefSeq; WP_015191516.1; NC_019748.1.
DR   AlphaFoldDB; K9XMV5; -.
DR   STRING; 111780.Sta7437_0226; -.
DR   KEGG; scs:Sta7437_0226; -.
DR   PATRIC; fig|111780.3.peg.234; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_036672_1_1_3; -.
DR   OMA; EHDHGMT; -.
DR   Proteomes; UP000010473; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
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   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:AFZ33843.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010473}.
FT   DOMAIN          90..352
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   REGION          370..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  43826 MW;  3F93C61482337D7C CRC64;
     MIKQYIKEIN AELIQLLGKK IDLLRGVQAP ASNAGVSPLQ EIKSNDDNES DIPSILNQAG
     VPQFVWQNLV INCQAAVKSR LPTNLQAKPR RVTIIGGGGM MGSFFAQKLS AAGHQVTILG
     HDDWDKAEEL LNDRDLVLIC VPIEYTTEVI QKTVKYLSPN TALADLTSIK TPALKTMLEY
     HSGAVIGLHP MFGKVQSFLS QKVVVCSGRR DEEFQWLLKL IEADGGELIH STAEEHDRMM
     VAVQAIRQFT TFSLGVFLAE QELDARRSLD FASPPYRLQL GMISRLLTQS APMVIDIMLA
     TTESRQAIGK LAATYARLAK LVKESRREEL IAEFGAIQAY LVPQMDCCLT ESHHVINALS
     NFLNGKRQET ENVGANRGSP LQKEEGRRQK AEASVF
//
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