ID G5GMW2_9FIRM Unreviewed; 296 AA.
AC G5GMW2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:EHG21890.1};
GN ORFNames=HMPREF9334_00593 {ECO:0000313|EMBL:EHG21890.1};
OS Selenomonas infelix ATCC 43532.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=679201 {ECO:0000313|EMBL:EHG21890.1, ECO:0000313|Proteomes:UP000004129};
RN [1] {ECO:0000313|EMBL:EHG21890.1, ECO:0000313|Proteomes:UP000004129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43532 {ECO:0000313|EMBL:EHG21890.1,
RC ECO:0000313|Proteomes:UP000004129};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas infelix ATCC 43532.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:EHG21890.1}.
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DR EMBL; ACZM01000004; EHG21890.1; -; Genomic_DNA.
DR RefSeq; WP_006692043.1; NZ_JH376797.1.
DR AlphaFoldDB; G5GMW2; -.
DR STRING; 679201.HMPREF9334_00593; -.
DR PATRIC; fig|679201.3.peg.597; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_0_1_9; -.
DR OrthoDB; 9802008at2; -.
DR Proteomes; UP000004129; 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; 3.40.50.720; 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}.
FT DOMAIN 4..293
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 296 AA; 31805 MW; 2BD9DC63CBC07970 CRC64;
MSGTKLAIIG VGLIGGSLGL CLKEALGDDI YITGLCRSEK SMRAAVECGA VDEASSDLAA
VVGDADIVYL SPPVLQIVPM VKKILPYLKD GVILTDAGST KGYVYEALHE ILPHTVYYVP
GHPMTGREKS GVEAATKNLF ANKAYVIIDD PQVPQAVKDR LMTILRLTGA KFTTLDLAQH
DRCAAVISHV PHLAAAALVT LLNRSGDDLD SCLKLIGGGF KDTTRIASSN ADMWADICMT
NGKPIADSLR QLQTILGEVI TAVEAEDRQA VHDYFIASKE RRDSILYDAE QKFDTN
//