ID A0A0J8QKA5_COCIT Unreviewed; 1076 AA.
AC A0A0J8QKA5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=CISG_03309 {ECO:0000313|EMBL:KMU72875.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU72875.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS268128; KMU72875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8QKA5; -.
DR STRING; 454286.A0A0J8QKA5; -.
DR Proteomes; UP000054559; 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:UP000054559}.
FT DOMAIN 714..977
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 120757 MW; AA8C748855F3EABC CRC64;
MSPADLTPQN GNGVPANGAN GLAPPSGSGT PLGFHRVHNK LLDSVKGTPA REPSPQPVHL
GIPGGSPRVL SEEGPGYVAA KFEGKGKQME QVMDQLEESG FIPSEFISTE TDWFYNMLGI
DDMYFQTETV DAIPSHILSL YAAKVAAYAR DDKRLDIRLD KEAADHAVYI DTSRPGVSAV
GGPRYEQRID EKYIDGSTPS NSYRVETFRS ATSLPDDNQH QLRCYFVYKC HFNNPHPDPG
ETNIEVIGEK RFLQKATENT KAIYQEIISN AVARSGPVIE MFEIEGSREK RLVVAYRQGS
AMGFFSALSD LYHYYRLTSS RKYLENFSNG ITVVSLYLRP IAGAEASGRH PPIEAAIHQI
MKEVSLLYCV PQNKFQSHFA SGRLSLQETI YAHCVWVFVQ QFLNRLGSEY TSLTALLDSN
NTVHAELLSK IKKRLRTETF TSDYILEIIN KYPELIHRLY LDFANTHYVQ TRAAGDDFLP
TLSYLRLQVD EVLDSKQLKD LVSKTVVSEH DEMVMKSFLV FNNAVLKPNF YTPTKVALSF
RLNPDFLPTH EYPQPLYGMF LVISSEFRGF HLRFRDISRG GIRIVKSRDK EAYAINARSI
FDENYNLANT QQRKNKDIPE GGAKGVILLD VNHQDKARVA FEKYIDSILD LLLPPVSPGI
KDPIVDLHGQ DEILFMGPDE NTAELVDWAT MHAKQRGAPW WKSFFTGKNP KLGGIPHDTY
GMTTLSIRQY VEGIYRKTGV DETQIRKLQT GGPDGDLGSN EILLGREKYT AIVDGSGVIV
DPQGLDREEL LRLAKARIMI SNFDMSKLSP EGYRVLVDDA NVTLPNGEVV HNGTVFRNTF
HLRKGDYDMF VPCGGRPESI NLANVSKLIV DGKTTIPYLV EGANLFLSQD CKLRLEKSGC
VLFKDASVNK GGVTSSSLEV LASLSFDDKG FAEHMCIGED GKAPEFYNAY VREVQETIKR
NATLEFEAIW REHELTGIPR SILSDTLSVA ITKLDEELQK SELWDNLRLR KAVLGDALPK
LLQEKIGLDT LLERVPDSYL RSIFGSYLAS RFVYQYGATP GQFAFFDFMS KRMPKE
//