ID I3R4D2_HALMT Unreviewed; 261 AA.
AC I3R4D2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:AFK19092.1};
DE EC=1.3.1.12 {ECO:0000313|EMBL:AFK19092.1};
GN Name=tyrA {ECO:0000313|EMBL:AFK19092.1};
GN OrderedLocusNames=HFX_1382 {ECO:0000313|EMBL:AFK19092.1};
GN ORFNames=BM92_02265 {ECO:0000313|EMBL:AHZ21548.1}, C439_03588
GN {ECO:0000313|EMBL:EMA04009.1}, E6P09_09935
GN {ECO:0000313|EMBL:QCQ75565.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK19092.1, ECO:0000313|Proteomes:UP000006469};
RN [1] {ECO:0000313|EMBL:AFK19092.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK19092.1};
RX PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT "Identification of the haloarchaeal phasin (PhaP) that functions in
RT polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT mediterranei.";
RL Appl. Environ. Microbiol. 78:1946-1952(2012).
RN [2] {ECO:0000313|EMBL:AFK19092.1, ECO:0000313|Proteomes:UP000006469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC {ECO:0000313|EMBL:AFK19092.1};
RX PubMed=22843593; DOI=10.1128/JB.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3] {ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000011603};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EMA04009.1, ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA04009.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000011603};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [5] {ECO:0000313|EMBL:AHZ21548.1, ECO:0000313|Proteomes:UP000027075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ21548.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000027075};
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AFK19092.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087;
RA Wang L., Yang H., Xiang H.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:QCQ75565.1, ECO:0000313|Proteomes:UP000299011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ75565.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000299011};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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; CP001868; AFK19092.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ21548.1; -; Genomic_DNA.
DR EMBL; AOLO01000003; EMA04009.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ75565.1; -; Genomic_DNA.
DR RefSeq; WP_004057123.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R4D2; -.
DR STRING; 523841.HFX_1382; -.
DR PaxDb; 523841-HFX_1382; -.
DR GeneID; 40156738; -.
DR KEGG; hme:HFX_1382; -.
DR PATRIC; fig|523841.21.peg.729; -.
DR eggNOG; arCOG00245; Archaea.
DR HOGENOM; CLU_077586_0_0_2; -.
DR OrthoDB; 24743at2157; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR Proteomes; UP000299011; 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; IPR046826; PDH_N.
DR InterPro; IPR003099; Prephen_DH.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 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:AFK19092.1}.
FT DOMAIN 1..261
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 261 AA; 27327 MW; B684BD57F786EF97 CRC64;
MDLLIVGAGA MGRWFGRTVD ADLAFADADP ERATAAADDL GGRAVPLDGD EQFDVVCLAV
PMRLAAEAVD ANAHRATDVM CDVTGSMAAP VAAMREHFDG HERLSLHPLF APQNGPGNVA
AVVDESGPLT DAILADLDSA GNHVFETTPE EHDRAMETVQ AATHAAVLSF GLAADNVRDE
FATPVSAALD ELVASVSGGT PRVYADIQSS FGDGTDRVAD AARALAMADP ETFADLYRTV
ARSDTSKDGN EHETDKHDPV E
//
