ID A0A0M0K7Q0_9EUKA Unreviewed; 1067 AA.
AC A0A0M0K7Q0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glu leu phe val dehydrogenase {ECO:0000313|EMBL:KOO34829.1};
GN ORFNames=Ctob_009836 {ECO:0000313|EMBL:KOO34829.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO34829.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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:KOO34829.1}.
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DR EMBL; JWZX01001077; KOO34829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0K7Q0; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000037460; 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: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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037460}.
FT DOMAIN 666..939
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1067 AA; 115517 MW; FA0CA8DE4CC9C3EC CRC64;
MERAAVVHWL KLRAASSDLD ALHDGVNSPN TAPWEGLALG MLKPQPEARP SVRQVQHTAA
VLVAAGTSTR PSSSRRLSSG IISLPDSTAV IAELATLQQR ASAREVPWFL ANMPQSYFRH
VSAPLRSKHL QAITAVCSDG VQVPDVMLKD GGEFTFLSSE TKQMGRTKTA AVARELDSLP
SGTDLQSVRL FSSKDGRLGL HLFSTVAEQE AEPRFAAATP EERAAEQVMH GYLSELLAGS
FTSEAAGRHT PPESSLTNRS AKASLDAFLR RCPSSYVTSH KPRLLLKQRH LCESIAGTDD
VAVDIERLPA SFALGEDEST LLTLATHGMS ARAALRRILA LLDVHGLNLY RAAVTIIDDR
PSDGACADAG TSIAPGSISL LEAEVAVGLA DLALAVVDHP IFTRPYVYET LLRPRVLPHA
NELARLFIRR FDPTDIFASA ALDTALLAAS EAREKSLEDE STRMLLRAME SAVRHTLRAN
VHRDARWALA LRLDPKFFAP KLPPAPSSVS NLPFGVFFCA GRSFNGYHTR FADIARGGLR
VVLPPSAEAH MAESSRHFKE CFDLAWAQHL KNKDIPEGGS KAVCLATPSV DGEERSKLLH
RCVKTFTDSL LDVLVVPHPT PAQPELLYLG PDENITPFDI NWIVARAKKR GYSMAPAFMS
SKPREGINHK VYGVTSEGVA VFLEHALRAI GIRPDAEPWS IKLTGGPDGD VAGNMLKVLA
RDYGDYVRVV GMADGSGCAE DPDGLPMADL LRLFHAGLPL SEMRTELLGP RGSLTLANTP
EGAALRNTLH NRVQADIFVP AGGRPAAING ANWKQYLLPD GSPSSRAIVE GANLFLTPEA
RAGLFGATGL PIVKDSSANK CGVICSSMEI VASMTLSADE FVDIKEQYVH DVLCRLRELA
GQEASLLFAE SARDPTVPHV KISEQISFAC LRVATALAAL LDRFDQSANK DRLWPLVREQ
LPPVLFEKYA ARLPERIPWE YQKSMIANGL ASRLVYREGL TFVNSVPDSA LPSFALAYLQ
QEQRVRALAA EVAKSGHDFA PEVSRLLLQG GVRAAAEEAA TRKAARA
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