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Database: UniProt
Entry: K9D4L3_9FIRM
LinkDB: K9D4L3_9FIRM
Original site: K9D4L3_9FIRM 
ID   K9D4L3_9FIRM            Unreviewed;       287 AA.
AC   K9D4L3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN   ORFNames=HMPREF9282_01412 {ECO:0000313|EMBL:EKU78131.1};
OS   Veillonella seminalis ACS-216-V-Col6b.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=883156 {ECO:0000313|EMBL:EKU78131.1, ECO:0000313|Proteomes:UP000009891};
RN   [1] {ECO:0000313|EMBL:EKU78131.1, ECO:0000313|Proteomes:UP000009891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-216-V-Col6b {ECO:0000313|EMBL:EKU78131.1,
RC   ECO:0000313|Proteomes:UP000009891};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Veillonella ratti ACS-216-V-COL6B.";
RL   Submitted (SEP-2012) 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:EKU78131.1}.
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DR   EMBL; AHAF01000011; EKU78131.1; -; Genomic_DNA.
DR   RefSeq; WP_006556299.1; NZ_JH992937.1.
DR   AlphaFoldDB; K9D4L3; -.
DR   STRING; 883156.HMPREF9282_01412; -.
DR   GeneID; 83055655; -.
DR   PATRIC; fig|883156.3.peg.1374; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_0_0_9; -.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000009891; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          3..287
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   COILED          241..268
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   287 AA;  31249 MW;  F084E2AC94C05D29 CRC64;
     MKRKVGIIGL GLLGGSLAKG LVQFTDYEVI GYARRSEICE QALADKTVTH AYKDPKEVVA
     EADILVFALP PDTNARLFEE LAPLIRPRTL ITDVSSTKTN FARTVKQYLP QGAKFVSIHP
     MAGSEKGGYG MAKADLFKNC TWIVLEDDVE SGWDAAAAAE LAEMGKLLGG RVEQIPMSVH
     DGFMATISHM PHMVAAMVAT IAGGDEFGDL RLRLAAGGFR DITRVAGGNP GMWREIITGN
     RTEVVRALSD LEQQISNIKN LLLTADDDTL ESYLNDAKHI RDKFSLL
//
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