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
//