ID I0ESP4_HELCM Unreviewed; 275 AA.
AC I0ESP4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:AFI05963.1};
DE EC=1.3.1.12 {ECO:0000313|EMBL:AFI05963.1};
GN OrderedLocusNames=HCD_04795 {ECO:0000313|EMBL:AFI05963.1};
OS Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163745 {ECO:0000313|EMBL:AFI05963.1, ECO:0000313|Proteomes:UP000005013};
RN [1] {ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 99-5656.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFI05963.1, ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RX PubMed=24358262;
RA Kersulyte D., Rossi M., Berg D.E.;
RT "Sequence Divergence and Conservation in Genomes ofHelicobacter cetorum
RT Strains from a Dolphin and a Whale.";
RL PLoS ONE 8:E83177-E83177(2013).
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DR EMBL; CP003481; AFI05963.1; -; Genomic_DNA.
DR RefSeq; WP_014659470.1; NC_017735.1.
DR AlphaFoldDB; I0ESP4; -.
DR STRING; 1163745.HCD_04795; -.
DR KEGG; hcm:HCD_04795; -.
DR PATRIC; fig|1163745.3.peg.1010; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_0_7; -.
DR OrthoDB; 9802008at2; -.
DR Proteomes; UP000005013; 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:AFI05963.1}.
FT DOMAIN 1..275
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 275 AA; 30517 MW; 7E75BBB6EE9A3B81 CRC64;
MQAGIIGLGL MGGSLGLDLQ ELGYFRNILG YDSNALHAQQ ALTLGLVDEC VEFEKILECD
VIFLAIPVEG IILCLQKMTS IKEEATIIDL GGAKHNIVKS VPQIIRKNFI AAHPMCGTEF
YGPKASVKGL YENALVILCD LEDSGAHQVK LAKEIFLGIK ARLVKMKSSE HDAHTAYISH
LPHVLSYALA NSVLKQKNPE TILSLAGGGF RDMSRISKSS PLMWKDIFKQ NRDNILEAIE
KCETEITQVK TWIKNNDDES LEKWMAQANK LQEFM
//
