ID A0A0P1ERM2_9RHOB Unreviewed; 270 AA.
AC A0A0P1ERM2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Arogenate dehydrogenase {ECO:0000313|EMBL:CUH53160.1};
DE EC=1.3.1.43 {ECO:0000313|EMBL:CUH53160.1};
GN Name=tyrC_2 {ECO:0000313|EMBL:CUH53160.1};
GN ORFNames=SHM7688_02612 {ECO:0000313|EMBL:CUH53160.1};
OS Shimia marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH53160.1, ECO:0000313|Proteomes:UP000054823};
RN [1] {ECO:0000313|EMBL:CUH53160.1, ECO:0000313|Proteomes:UP000054823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH53160.1,
RC ECO:0000313|Proteomes:UP000054823};
RG Swine Surveillance;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYPW01000027; CUH53160.1; -; Genomic_DNA.
DR RefSeq; WP_058240346.1; NZ_FOMU01000002.1.
DR AlphaFoldDB; A0A0P1ERM2; -.
DR STRING; 321267.SHM7688_02612; -.
DR OrthoDB; 9800497at2; -.
DR Proteomes; UP000054823; Unassembled WGS sequence.
DR GO; GO:0047794; F:cyclohexadienyl dehydrogenase 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CUH53160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054823}.
FT DOMAIN 19..270
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 270 AA; 29201 MW; F2C8CC735F5A968B CRC64;
MGLKQTFERA HSVEQAQQPS VGLVGFGGFG RLIARELAQG NKLTICDPLY SRAVLPDGQR
LTLQGLAEVA QSDIVILAVP VSAMAHVCRV LAPHLRPGTL VVDVGSVKVA PMQDMQRLLP
AHVEILGTHP LFGPQSARSG IAGHKIALCP VRGSKWRRVA AVLRRRGLQV LVTSAQDHDR
ELAVVQGLTH MIGKVLSDLG PMPERLTTAS FDLLREAVRM VQDDPPTVLH AIEVANPYAA
EVRNAFFERA EELKAQFEAH PEVGQTVPAS
//