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Database: UniProt
Entry: A0A151BXI4_9MICO
LinkDB: A0A151BXI4_9MICO
Original site: A0A151BXI4_9MICO 
ID   A0A151BXI4_9MICO        Unreviewed;       358 AA.
AC   A0A151BXI4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE            EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN   ORFNames=AZH51_03445 {ECO:0000313|EMBL:KYH44699.1};
OS   Branchiibius sp. NY16-3462-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Branchiibius.
OX   NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH44699.1, ECO:0000313|Proteomes:UP000075667};
RN   [1] {ECO:0000313|EMBL:KYH44699.1, ECO:0000313|Proteomes:UP000075667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH44699.1};
RA   Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT   "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT   sample.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC         NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001162};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005067}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007964}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYH44699.1}.
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DR   EMBL; LVCF01000033; KYH44699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BXI4; -.
DR   STRING; 1807500.AZH51_03445; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000075667; Unassembled WGS sequence.
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:UniProtKB-UniPathway.
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; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075667};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT   DOMAIN          1..281
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   DOMAIN          291..358
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   358 AA;  36622 MW;  1FE950B7E082FC1E CRC64;
     MKVHVIGTGL IGTSIALALT RIGDEVTLED PSPTAAALAA DLGAGTVARP EHPDVVVVAA
     PPDVAAKVVE LALLTWPLAV VTDVASVKGA ILSDLLAYGE ADLTRYVGSH PMAGKERSGA
     VAAQADLFEG RTWVVCPAPH SAVSSVDLVA RLAASTGAAV VQMPADEHDA AVAAVSHVPQ
     LAASLVAARL RELPDGAIAL SGQGIRDVTR IAASDPLLWT QILSGNAAAI APVIDDLADD
     LSRVAQALRT LLSDDDGSGA RGVLARAIAD GQLGQARIPG KHGSAPTTYA ILTVIVPDEP
     GSLARLFNDM GDAGINLEDL RLEHGVGAKI GLAEVMVLPA VADRLRGVLE EKGWRVHD
//
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