ID C4JF29_UNCRE Unreviewed; 1086 AA.
AC C4JF29;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=UREG_00930 {ECO:0000313|EMBL:EEP76082.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP76082.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(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; CH476615; EEP76082.1; -; Genomic_DNA.
DR RefSeq; XP_002541415.1; XM_002541369.1.
DR AlphaFoldDB; C4JF29; -.
DR STRING; 336963.C4JF29; -.
DR GeneID; 8441750; -.
DR KEGG; ure:UREG_00930; -.
DR VEuPathDB; FungiDB:UREG_00930; -.
DR eggNOG; KOG2250; Eukaryota.
DR HOGENOM; CLU_005220_0_0_1; -.
DR InParanoid; C4JF29; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000002058; 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:UP000002058}.
FT DOMAIN 724..987
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 122422 MW; B923E8F83A4B1444 CRC64;
MSAAELTMNP APHAADGANG ASQPKVSPLP TAELSGSATP TTGFHRIHNK QLDGVMRTPG
RQPSPQPVHL GIPGGTHRVL SEQGPGYVAA KFEGKAKQME QVMDQLEESG FIPAEFISTE
TDWFYKMLGI DDMYFQTETV EAIASHILSL YAAKVAAYAR DDKRLEIRLD KEAADHAVYI
DTSRPGVSAV DGPRYEQRID EKYIDGSTPS NSYRVETFRS STSMPDENQN QLRCYFVYKC
QFNNPTPDPG ETNIEVIGEN RFLQKATANT KAIYQEIIIK AVARSGPVIE MFEIEGTRER
RIVIAYRQGS AMGMFSALSD LYHYYRLTSS RKYLENFSNG ITVLSLYLRP MPGVEASGRH
PPIEASIHQI MKEVSLLYCI PQNKFQSHFA SGRLSLQETI YAHCVWVFVQ QFLNRLGSEY
TSLTALLDSN NTVHAELLSK IKKRLRTETF TSDYILEIIN KYPDLIHRLY LDFASTHYVQ
TRAAEDDFLP TLSYLRLQVD EVLDSKQLKD LVSKTVVSEH DEMVMKSFLV FNRAVLKTNF
YTPTKVALSF RLNPDFLPSH EYPQPLYGMF LIISSEFRGF HLRFRDISRG GIRIVKSRDK
EAYSINARSI FDENYNLANT QQRKNKDIPE GGAKGVILLD VNHQDKARVA FEKYIDSILD
LLLPPASPGI KDPIVDLHGQ DEILFMGPDE NTAELVDWAT LHARQRGAPW WKSFFTGKNP
KLGGIPHDTY GMTTLSIRQY VEGIYRKMGV DETQIRKLQT GGPDGDLGSN EIFLGREKYT
AIVDGSGVIV DPQGLNRDEL LRLAKSRLMI SNFDSSKLSP EGYRVLVDDA NVKLPSGEVV
HNGTVFRNTF HLRHGNYDMF VPCGGRPESI NLANVSKLIV DGKSTIPFLV EGANLFLTQD
CKLRLEKAGC VLFKDASVNK GGVTSSSLEV LASLSFDDES FEQHMCIGEN GQAPEFYNAY
VREVQETIKR NATLEFEAIW REHEQTGIPR SILSDTLSVA ITKLDEELQK SELWENLRLR
KAVLGDALPK LLQEKIGLEV MLERVPDNYL RSIFGSYLAS RFVYQYGSTP GQFAFFDFMS
KRMPKE
//
