ID H9UL45_SPIAZ Unreviewed; 263 AA.
AC H9UL45;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:AFG38238.1};
GN OrderedLocusNames=Spiaf_2202 {ECO:0000313|EMBL:AFG38238.1};
OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38238.1, ECO:0000313|Proteomes:UP000007383};
RN [1] {ECO:0000313|Proteomes:UP000007383}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC {ECO:0000313|Proteomes:UP000007383};
RX PubMed=23991249; DOI=10.4056/sigs.3607108;
RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT Rift.";
RL Stand. Genomic Sci. 8:165-176(2013).
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; CP003282; AFG38238.1; -; Genomic_DNA.
DR RefSeq; WP_014456221.1; NC_017098.1.
DR AlphaFoldDB; H9UL45; -.
DR STRING; 889378.Spiaf_2202; -.
DR KEGG; sfc:Spiaf_2202; -.
DR PATRIC; fig|889378.3.peg.2178; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_036672_3_0_12; -.
DR OrthoDB; 9802008at2; -.
DR Proteomes; UP000007383; Chromosome.
DR GO; GO:0033730; F:arogenate dehydrogenase (NADP+) activity; IEA:InterPro.
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; 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 InterPro; IPR045011; TYRAAT1/2.
DR PANTHER; PTHR43207:SF4; AROGENATE DEHYDROGENASE 2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43207; AROGENATE DEHYDROGENASE-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000007383}.
FT DOMAIN 1..263
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 263 AA; 28583 MW; 077109C9688232FB CRC64;
MQIGVIGLGR FGMFWAQLLA QEAEAVYAWN RTPRALPAGV LPLGDADYQR LDIVFLCTSI
ASVGSVAETI ASRLHPRTIV ADTCSVKVEP LADLDRVIPA ENPLLGTHPM FGPDSARNGA
DGLPMVFSPV RIAPDQLAMV QDFFRKYQLD QLVMTPEEHD REAAYTQGIT HFIGRVLKDL
DLKPSPIATL GYTRLLQVME QTCNDPWSLF MDLQQRNPYT AAMRRDIRVS LDRTLQLLGD
SDAGGDAAAN AGPGADSGAA SSD
//