ID W6KSX1_9TRYP Unreviewed; 1005 AA.
AC W6KSX1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-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=GSEM1_T00006011001 {ECO:0000313|EMBL:CCW65295.1};
OS Phytomonas sp. EM1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW65295.1, ECO:0000313|Proteomes:UP000027080};
RN [1] {ECO:0000313|EMBL:CCW65295.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW65295.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW65295.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW65295.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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DR EMBL; HF955104; CCW65295.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KSX1; -.
DR EnsemblProtists; CCW65295; CCW65295; GSEM1_T00006011001.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000027080; 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; 3.40.50.720; 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:UP000027080}.
FT DOMAIN 619..900
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1005 AA; 113207 MW; 4BB8717A5EB9CF2E CRC64;
MMRRIAFRVA AVSRPVTVSA SVLPSMYRGV STTPTLEMDK IMSKIKSEGI FDTPMIKDTL
SRFVNSLSST TYLKHVTPEE VSNHVLGVLN AEASQKMGNA YEFAREDNHS AFYICKNEPE
SIIRNVRRMA KYTSRPDIPE NHSVVVRSFH AENPSMVIYT VSFVPFDVPK PDESETKAEK
LIPKQLLKNL SEEKLKRLQR LLDRRPNSVF PVIDTVEDSR SKDTILFTMA TCADKTNYIV
SLLNVFQEIK GSEVIRVSTC TLVSGDRVYS MIIKGATLEQ VKEQASMVGL LSSKAAKPIV
RMYESGMLTC EQAVYIDAAF IFSFYFTQIP VDDTYRHLRT VLENVPHGIN WLNSMRNSLA
QETMSEHYMG SLIENYPQFV QLIYEDFQKG STAERRASIA EQIVQKLADD GRLPHDVAIF
MSLLKFNEVV LKHNFFKTEK AALAFRLDPS FLKDLEYPLV PHGVFLFAGG HWRGFHIRFT
DIARGGVRLI VSKPNTYSKN KRTVFQENYN LAFTQLLKNK DIPEGGSKGT ILVSSRFLTA
FDEAACKRIF LQYVDAMLDL MIPGEPGIVN RLGQDEIIFL GPDEYTAGSF PSAGALHSKK
RGYVNWKSFT TGKDPDMGGI PHDVYGMTTR SVRTFVNAIY RELGLDGSKM RKFQTGGPDG
DLGSNEILMS NEVLIGVVDG SASLHDPNGL NREELLRLAC GRMPLAKFDR SKLSKDGFLV
LVDDVNVTLP DGTLVKKGVQ LRDEFHFLKY SDADVFVPCG GRPRSITLEN VARLLKMKGV
DGEDMLQGRV NPTPSQLKYK IIVEGANLFI SQDARLALER CGVVLIKDAS SNKGGVTSSS
LEVFAGLCLS DEEHAKYMCV RDELNPPLFY KRLVEEIVAR IEKNAENEFN AIWSEWKKDP
SKPKTLIADA LSSKSVKIRA DILKSDIFAD KKLVRHVMME YAPKTLLEVV PIDKMLQRVP
EVYQHAICAM WLSSNYVFSG RANSNEFDFF KFLTEEIKRM NAKYE
//