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Database: UniProt
Entry: H9UL45_SPIAZ
LinkDB: H9UL45_SPIAZ
Original site: H9UL45_SPIAZ 
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).
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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
//
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