ID G8B7E8_CANPC Unreviewed; 1055 AA.
AC G8B7E8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN OrderedLocusNames=CPAR2_104190 {ECO:0000313|CGD:CAL0000151747,
GN ECO:0000313|EMBL:CCE40382.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE40382.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
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).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
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; HE605203; CCE40382.1; -; Genomic_DNA.
DR AlphaFoldDB; G8B7E8; -.
DR STRING; 578454.G8B7E8; -.
DR EnsemblFungi; CPAR2_104190-T; CPAR2_104190-T-p1; CPAR2_104190.
DR CGD; CAL0000151747; CPAR2_104190.
DR VEuPathDB; FungiDB:CPAR2_104190; -.
DR eggNOG; KOG2250; Eukaryota.
DR Proteomes; UP000005221; Chromosome 1.
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:UP000005221}.
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; 118980 MW; 0DEA3AE4203D5F36 CRC64;
MTSLEQGVAN LNIYKSNSTS NNSSAVSLKH DYIDSPFSGK KDQFDQVLDA LDSTGFIPES
LLESEAKWFY ESLGIDDVFF ARSTPEEIAG HIHALYSCKV QAYANAGEQP LISYKREAED
HAVFFDTVDA LDYARNPFES LIDDKYIDPS DAANKSYRAE YFAAPLNYQT DPILNGIYAQ
NKNLGEQIVR LVFVYKNQFK NEKVATDELD LDKIGDETFL KIASQNTKSL YESINKEVIK
STGPIIKHFQ IENSDEYRVI IGYRQSTAAR YNSALSDLAN YYKLQTTRKY VEQFANGVTI
TSMYVTSRSR SAVDLSIYQV IKEASLLYCI PHNFFHTRFI QGDLSLQESI YAQSGVIFVT
HFLNRLGPEY KKLSSLLDPS KSTEHAEVLS SLKKRLRSET YTQDYIKEVF DVRSEIVRKL
YRQFADVHYI RSSMEKTLSY QRLSQIQPVG SEEEFEQLLS RECSQNEHHA IVLRALYTFN
KSILKTNFYT STKVALSFRL DPSFLPETEY PERPYGMFFV VGSDFRGFHI RFRDIARGGI
RIVRSRNLDA YNVNARNLFD ENYNLANTQQ RKNKDIPEGG SKGVILLDSG SAQDRAQASF
EKYIDALIDL LLKQHIPGVK DNYVDLYNKP EILFLGPDEG TAGYVDWATL HARERGAPWW
KSFLTGKSEA IGGIPHDEYG MTTLSVRAYV NKIYEKLNID NSKIRKFQTG GPDGDLGSNE
ILLSRDEIYV GIVDGSGVIA DPNGLDKQEL IRLAKSRKMI DHYDRSKLSP QGYIVLVDDF
DVTLPSGQVV TSGVAFRNTF HLKLKEQFGT NGVDLFVPCG GRPAAIDTNN VHELIDEKTG
KSIIPYFVEG ANLFITQSAK LVLEKAGTII FKDASTNKGG VTSSSLEVLA ALAFDDKGFL
ENMCVDTKTG EKPQFYQKYV KDVQNKIVAN ANSEFEALWK LKAETGIPFT ILSDKLSLAI
NKLGDELANS KELWDDDVDF RNAVLLDSLP PLLLSTVGIE NVLARVPQAY LKAIFATYLA
SHFVYSRGID SNPAKFLEFI SNLRKGFVQK GLLKY
//
