ID D4J8J4_9FIRM Unreviewed; 365 AA.
AC D4J8J4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=CC1_19340 {ECO:0000313|EMBL:CBK80665.1};
OS Coprococcus catus GD/7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK80665.1, ECO:0000313|Proteomes:UP000008798};
RN [1] {ECO:0000313|EMBL:CBK80665.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK80665.1,
RC ECO:0000313|Proteomes:UP000008798};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Coprococcus catus GD/7.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK80665.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK80665.1,
RC ECO:0000313|Proteomes:UP000008798};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929038; CBK80665.1; -; Genomic_DNA.
DR AlphaFoldDB; D4J8J4; -.
DR STRING; 717962.CC1_19340; -.
DR KEGG; cct:CC1_19340; -.
DR PATRIC; fig|717962.3.peg.1772; -.
DR HOGENOM; CLU_055968_2_1_9; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000008798; 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: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 ECO:0000313|EMBL:CBK80665.1};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 4..291
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 296..365
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 365 AA; 40327 MW; D81B7819314C9F64 CRC64;
MSDKTIGFIG LGLIGGSIAK ALRRVHPEYR LIAYNRSRSS LVEAMSDGTI NQATDVIDAS
FAECDFIFLC MPVSVNIQCL KKLKDLVPDT CVITDVGSVK STIHEAVREL GMEARFIGGH
PMAGSEKTGY TSATDRLLEN AYYIITPTAL SNPDKVAEMR QLVTDTGAVP IVLNCEEHDY
ATAAISHLPH VIAYTLVNLV RTSDSREGLM RQLAAGGFKD ITRIASSSPD MWESICLENQ
GQLLKVIDAY KASLEDISEA IRENLGDKLH CFFEEAKDYR DSMPMKMKGS IEPAYEIYVD
LIDESGAIAT IATILASNRI SIKNIGILHN REFQEGVLRI EFYEQDAVEK ATALLSKYSY
IIHTR
//
