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
//