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Database: UniProt
Entry: S5YS88_PARAH
LinkDB: S5YS88_PARAH
Original site: S5YS88_PARAH 
ID   S5YS88_PARAH            Unreviewed;       322 AA.
AC   S5YS88;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:AGT08071.1};
DE            EC=1.3.1.12 {ECO:0000313|EMBL:AGT08071.1};
GN   ORFNames=JCM7686_0962 {ECO:0000313|EMBL:AGT08071.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT08071.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT08071.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT08071.1};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(2014).
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DR   EMBL; CP006650; AGT08071.1; -; Genomic_DNA.
DR   RefSeq; WP_020949709.1; NC_022041.1.
DR   AlphaFoldDB; S5YS88; -.
DR   STRING; 1367847.JCM7686_0962; -.
DR   KEGG; pami:JCM7686_0962; -.
DR   PATRIC; fig|1367847.3.peg.925; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_0_1_5; -.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000015480; Chromosome.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
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: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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AGT08071.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480}.
FT   DOMAIN          6..295
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   REGION          293..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  34296 MW;  0605D337507654E1 CRC64;
     MSVIYDRVAL IGLGLIAGSM SLAMRQAGLV REVVGYARSA ETRATAAEIG LVDRVTDSAA
     DAVRDADLIV LAVPVGAMGE IAAEIAPFLK KGAVVTDVGS VKQAVIEAVA PHIPEGVHFI
     PSHPLAGTEH SGPRSGFASL FSNRWWLLTP PEGADRAEVD RLASLIRGIG ANVEDMDAAH
     HDTVLAVTSH TPHLIAYTMV GVADHIKRVT ESEVIKYSAA GFRDFTRIAA SDPTMWRDVF
     LQNKEAVLDI LGRFAEELFV LQRAIRMGDG QHLHDYFTRT RAIRRGIIEA GQDTAAPDFG
     RSPGAAAPDA AKPEPAKAAG QD
//
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