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Database: UniProt
Entry: H1L082_9EURY
LinkDB: H1L082_9EURY
Original site: H1L082_9EURY 
ID   H1L082_9EURY            Unreviewed;       442 AA.
AC   H1L082;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:EHP85133.1};
GN   ORFNames=MetfoDRAFT_1456 {ECO:0000313|EMBL:EHP85133.1};
OS   Methanotorris formicicus Mc-S-70.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanotorris.
OX   NCBI_TaxID=647171 {ECO:0000313|EMBL:EHP85133.1, ECO:0000313|Proteomes:UP000003706};
RN   [1] {ECO:0000313|EMBL:EHP85133.1, ECO:0000313|Proteomes:UP000003706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mc-S-70 {ECO:0000313|EMBL:EHP85133.1,
RC   ECO:0000313|Proteomes:UP000003706};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Sieprawska-Lupa M., Takai K., Miyazaki J.,
RA   Whitman W., Woyke T.J.;
RT   "The draft genome of Methanotorris formicicus Mc-S-70.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHP85133.1}.
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DR   EMBL; AGJL01000039; EHP85133.1; -; Genomic_DNA.
DR   RefSeq; WP_007044885.1; NZ_AGJL01000039.1.
DR   AlphaFoldDB; H1L082; -.
DR   STRING; 647171.MetfoDRAFT_1456; -.
DR   PATRIC; fig|647171.4.peg.1419; -.
DR   OrthoDB; 24743at2157; -.
DR   Proteomes; UP000003706; Unassembled WGS sequence.
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; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR   Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding 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; IPR005121; Fdx_antiC-bd.
DR   InterPro; IPR036690; Fdx_antiC-bd_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR008299; Prep_DH/arog_DH.
DR   InterPro; IPR003099; Prephen_DH.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF03147; FDX-ACB; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   Pfam; PF02153; PDH_N; 1.
DR   PIRSF; PIRSF006549; PDH_arog_dh_reg; 1.
DR   SMART; SM00896; FDX-ACB; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 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}.
FT   DOMAIN          4..286
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   442 AA;  50835 MW;  C1B97729CC10C454 CRC64;
     MKNYKVSIIG GTDGLGKWFA KYLKSKNFDV TVTGRDIVKG KSVEKELGVK FTNNNIEAAK
     EGDIVIVAVP INVTERVIRE VAPHVREGCL LMDITSIKEI PSKTMEEYAK EGVTVVPTHP
     MFGPSTPSLM RQVVILTPSE RHKKSEWFRK VKDFLEKEGA RVIVIKPEEH DRIMGVVQGL
     THFAYISLGA TLKELGVDIK ESRKYASPIY ELMIYIIGRI IGQNPYLYAD IQMHNPQIKH
     IHETFIGQCN LIKNIVERKD REEFVKLMKE AAKHFGNEAK RGVSYSDKAV FALTKEMEKL
     SKMKGKDIGL RHIYSGNVHY GILKDVDGDY IIIEKNGKEI KLSTSNVMVM EENELKKWKD
     ENLPKYHRDV SILFKKDVDE NVILDLLKDR FDVEIMDIYE GEKIEEGFKS VTFRVYAFEN
     VEEKEREFLK IIENIGGKRR FK
//
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