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
//