ID A0A024GGR7_9STRA Unreviewed; 1013 AA.
AC A0A024GGR7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal domain-containing protein {ECO:0000259|SMART:SM00839};
GN ORFNames=BN9_070110 {ECO:0000313|EMBL:CCI46082.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI46082.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI46082.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI46082.1,
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:CCI46082.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAIX01000116; CCI46082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GGR7; -.
DR STRING; 65357.A0A024GGR7; -.
DR InParanoid; A0A024GGR7; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 642..914
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1013 AA; 114829 MW; 221BC1948C5C0430 CRC64;
MTQQMAALTQ KNKVREHIQL DGLFTQESIE REVEWFYGPL GLHDFYFIGQ SPENIAKHIQ
SIIAAKLVSK ASGRPMDIKL EQHSENEAFF AARSNVQGES TTRQCSENCP TEVEQLELQI
EKQYLSGSAQ EWIGDGVRSG YQFLEPNEAV KTQKSHYRLQ CYRSVGVLDP TIVPYHVRMY
FLQKPDFVDP NPSTSETSIQ KLADKTFLSR AGDNLKRVYQ ECLTQAVEQM TPVFHTEIWK
EKDQVEMARV TIAYKSGSTH GYFSSIADLY RQLGLFSTRK YVEFFSNGYV IYAFYLQQLQ
NSQKCDISLA KQIEMLVADA SLHFVLPRTS LTPMLRNGLL APKPIAYAYA AWKFVFHFMH
RLPDAYTVVA TSLRGHDSSA MARLEQLRTT MKVNTYTESQ ILEHILQSSS IVKLLYNEFE
SLHAPQTGNN PPSTASTLSA LRKSTNSEQA LLIFSLFHTF NKNTTKTNFF LKDKSALSFR
LDGEFLSETE YSEKPFAIIY VIGSEFRGFH VRFSDIARGG IRMIRSSHAQ VYLNNVSSLF
DECYSLASTQ QRKNKDIPEG GSKGVILLNQ AHQDKADIAF QKYIDALLSI MLQKINGEEE
LLFLGPDEGT AHMMDWASLY AKKRGYSYWK AITTGKSATH GGIPHDVYGM TTHSVRQYIK
GIQRKLNLDQ KGAKRITKVQ TGGPDGDLGS NEIKMSGDEC TIAIVDGSGV LYDPEGLDRS
ELQALAEKRE PISSFDSHKL TPNGYQVLVT QNDVRLANGE IIENGVEFRN LYHLRPSLSA
DFFVPCGGRP SAVNLNNVEE FLYQSDGKSL RFRYIVEGAN LFFTQDARLR LEQAGVILFK
DASANKGGVT SSSLEVLAAL CMSDQEFEEN MQVDAMTGKK PAFYEEYVKE VQLRIARNAS
QEFECLWREH ERTKIPFSVL SNHLSERITK LSVEIQDSIL WDNVQLRELV LRQGIPALLH
EKIGFGNFVA RLPEKYTRAL FASQIASRFV YSVGLHAREF AFYEFLSEFM QSR
//
