ID C4LGN4_CORK4 Unreviewed; 345 AA.
AC C4LGN4;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:ACR16989.1};
DE EC=1.3.1.12 {ECO:0000313|EMBL:ACR16989.1};
GN OrderedLocusNames=ckrop_0197 {ECO:0000313|EMBL:ACR16989.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR16989.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR16989.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001620; ACR16989.1; -; Genomic_DNA.
DR AlphaFoldDB; C4LGN4; -.
DR STRING; 645127.ckrop_0197; -.
DR KEGG; ckp:ckrop_0197; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_1_0_11; -.
DR Proteomes; UP000001473; 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:ACR16989.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT DOMAIN 27..329
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 36963 MW; F035D3AA39B16839 CRC64;
MSISTPSGVY PDPATTPGKH HILHEDRPVC ILGLGLIGGS IMRDVQARGR RVFGWDRTQS
TVTNIIDDGF DASNDCSAVL ERAEDEDALV VIATPMSAVG TMLDRVVEHA PTCGITDVVS
VKQAVIREVR ARGMHDRFVG GHPMSGTSHN GWEASQTGLF TGAPWVVTFD NAPTNDGDGG
RWLREWMSVV NLAYDVGAEV VPARAQSHDA AVARISHLPH VLADALAVAG DSGGALALSL
AAGSFRDGTR VASSDPELTE AMCENNVKEV LRAIEEVQTM LDEARESLRA TPPSVAELAD
AGHRSRIRYE ARTGKRPVLR LHPGDAGWVD QLKQAENLGA RIEVF
//
