ID C5M741_CANTT Unreviewed; 1055 AA.
AC C5M741;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=CTRG_01673 {ECO:0000313|EMBL:EER34811.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34811.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER34811.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC glutamate to ammonia and alpha-ketoglutarate.
CC {ECO:0000256|PIRNR:PIRNR000184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC Evidence={ECO:0000256|PIRNR:PIRNR000184};
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000184}.
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DR EMBL; GG692396; EER34811.1; -; Genomic_DNA.
DR RefSeq; XP_002547366.1; XM_002547320.1.
DR AlphaFoldDB; C5M741; -.
DR STRING; 294747.C5M741; -.
DR EnsemblFungi; CTRG_01673-t43_1; CTRG_01673-t43_1-p1; CTRG_01673.
DR GeneID; 8301490; -.
DR KEGG; ctp:CTRG_01673; -.
DR VEuPathDB; FungiDB:CTRG_01673; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_005220_0_0_1; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniRule.
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 InterPro; IPR016210; NAD-GDH_euk.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR PIRSF; PIRSF000184; GDH_NAD; 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 NAD {ECO:0000256|PIRNR:PIRNR000184};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 673..946
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1055 AA; 119946 MW; 2C07F020F324F28D CRC64;
MTTSLENGVS HLNIYKTTSN TSSQISLKHD YIDSPFSGKK DQFEQVLDVL DSTGFIPESL
IESETKWFYE SLGIDDVFFA RSSPEDIASH IHALYSCKVQ AYSSFGEQPL ISYKRESDDH
AVFFDTVDAE NYKRNQFEER IDDKYIDPSN STTNSYRTEY YSAPLNYQVD PILSGVYQQN
SELRNQFVRL FFVYKNQYIQ AQVDKNETDL EKIGDKTFLQ IASDNTKNLY TSIVKDVINT
TGPVIRHFPI EDSEEYRVVI GYRQNSTARY NSALGDLANY YKLHVTRKYV EQFANGVTII
SMYVTSKSRK SPVDLSIYQV IKEASLLYCI PHNFFHDRFI QGELSLQESI YAQSGVIFVT
HFLNRLGPEY SKLSSLLDPS KSIEHAEVLN SLKKRLRAET YTQDYIKEVF DTRRDIVRKL
YRQFADVHYI RSSMEKTLSY QRLSQITPVG SEEEFEKLLS RECSQNEHHA VVLRALYTFN
KSILKTNFYT STKVALSFRL NPSFLPESEY PERPYGMFFV VGSDFRGFHI RFRDIARGGI
RIVRSRSLDA YNVNARNLFD ENYNLANTQQ RKNKDIPEGG SKGVILLDHG SAQERPQACF
EKYIDALIDL LLKQHIPGVK DSYVDLYQKP EILFLGPDEG TAGYVDWATL HARERGAPWW
KSFLTGKSPE IGGIPHDEYG MTTLSVRAYV NKIYEKLNID DATIRKFQTG GPDGDLGSNE
ILLSRKENYV GIVDGSGVIA DPQGLDKQEL LRLAKERKMI EHYDRSKLSP QGYIVLVDDM
DVKLPSGDIV TSGVAFRNTF HLKLKEQFGT NGVDLFVPCG GRPAAIDTNN VHELIDEKTG
KSVVPYFVEG ANLFITQSAK LILEKAGIII FKDASTNKGG VTSSSLEVLS ALAFDDKGFL
DNMCVDPKTG AKPQFYQDYV KDVQKIIVRN AEAEFESLWK LKAETGTPFT ILSDKLSVAI
NKLGDELANS KELWEDDIEF RNAVLLDSLP PLLLEKVGIE NVLARVPEAY LKAIFATHLA
SKFVYSRGID SNPAKFLEFI SSIRKEFVKK GLLKY
//
