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Database: UniProt
Entry: A0A024GDG4_9STRA
LinkDB: A0A024GDG4_9STRA
Original site: A0A024GDG4_9STRA 
ID   A0A024GDG4_9STRA        Unreviewed;      1075 AA.
AC   A0A024GDG4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal domain-containing protein {ECO:0000259|SMART:SM00839};
GN   ORFNames=BN9_055570 {ECO:0000313|EMBL:CCI44733.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI44733.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI44733.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI44733.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382}.
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:CCI44733.1}.
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DR   EMBL; CAIX01000078; CCI44733.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GDG4; -.
DR   STRING; 65357.A0A024GDG4; -.
DR   InParanoid; A0A024GDG4; -.
DR   OrthoDB; 89313at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF24; GLUTAMATE DEHYDROGENASE 2; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT   DOMAIN          682..932
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   COILED          1037..1064
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1075 AA;  120147 MW;  CCAB21B7DC1AF365 CRC64;
     MTLLLKIRVS ASASALHAHA KRSLVQRRSN LFKCYLNTQV HESPEDLLQA LTKHQHDAAT
     KTVPWFLENM PAAYFRAIGQ EERLQHLNAV TALVHAQQPE VMLRSSDHKV YSYIRTGANH
     PKVLPNVLSM LPKSIKGGAE LARVKIFTSL DDTLGLEIFR YGFQGQCCFP IHSISSSPFD
     RITEPFTGTT EQEKSAYAKI QEFCAKIQSG VFKGKEYYPE PAAYFEPDQV DEFLHRCNSM
     YVCFSNPRRI AAQMALFHRV RGTEGVVVDI EHGWQTRSDE NKLSGGTLPQ TMLTIAGANV
     VAKSMIQKAA TYLALCDLNV IRAHLDIVND HKAGNGHVAM IRILVTPHKE SSKESNWDQI
     VADLKYLKWI DDQPIELCRK YPNVQLQSSE IIYAYANMLH GMLAKKDPFA YSLDRIGTVV
     THPQQLPIAV AIANFFLRKF DPTQPKLSTD EIQNRAKALR NDIRSNVEAE DAIWLLNTMV
     DAVVGTLRTN RFVQSRYALA LRMDPSIVGH GTVGKDTPFG VFYVYGRRFK GFHVRFRDIA
     RGGLRVVYPN STDAHALESA RQYNEAYNLA FAQQLKNKDI PEGGSKAVVL CDPIVGLRGD
     SGLRDFVIRK SIKAFTDALL DLNTTDTNVR NRIVDYYERE ELIYLGPDEN IIPSDITWMT
     KRAASRGYPI PRAFISSKPD AGINHKTYGV TSEGVAVFAD VALRSQNIDP TSQPFTVKIT
     GGTDGDVAGN IIKILDRQYG KNVRVVGICD GTGSLENPDG LDMKELLRLV ETSQPLAAYN
     VDTLGVNGVF SSADTPQGIR ARNSMHNRIR SDLFIPAGGR PNTINENNWR EYLTPSGKPS
     CRLIVEGANL FITPEARQLL FDHAGVVIVK DSSANKCGVI CSSYEIIASM LLETEEFLHV
     KSELVAQVVD KLRQLACVEA ELLFREYKKN PNVALPPCSE RISRAIIRVH DAILQAFDDL
     SSDDQKVLMT LVQEHLPLKL QELALTRVES NVPRAYLKCI VASSLASKIV YREGLQYTED
     LPQSNLANLA LQYFKQEKKV RQLIENLNNS NTAQKEEIQD LLFRGGVRAG IDRAV
//
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