ID A0A165HKI6_9BASI Unreviewed; 1070 AA.
AC A0A165HKI6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=CALCODRAFT_493766 {ECO:0000313|EMBL:KZT59411.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT59411.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT59411.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT59411.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV423941; KZT59411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165HKI6; -.
DR STRING; 1353952.A0A165HKI6; -.
DR InParanoid; A0A165HKI6; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000076842; 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:UP000076842}.
FT DOMAIN 707..969
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 155..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 119642 MW; 06DB35B06B690248 CRC64;
MSHPEVVEPV ADSERSALLA NPNNAHLVGS NGHLSVPGTP YSLSSTRTGS DTSVNRIKNL
PGYKNYNFAG KSAQQDEVED NVASKGFIPA ELVNNEVVWF YHHLGIDDTY FANESVEVIS
DHILALYGAK LLAYTKHDPA KLVIDLEKIT KEGESDKSPE GAVFIHTSPP GKKATVGPGA
SCEKRIDNLY LDSSTVEKAY RLETYRSQGS VSATAGQQLR CYFVTRCQFP GTPAQKLPDG
TTDIRSVSDK RFLEKASEHT LDIYQFVMSN VETRYGPVIE VYEVEGTREM RVVIGYRMGG
TAHYFSALSD LYHFYGLYSA RKYVEQFANG VTIISMYLNP VPNSQAPPIE HSIYQVKKEA
SLLYCLPDNP FFAEEGIPHA VQEATYAYSG WIFAQHFCNR LGAAYLALKN VLDETNPSHE
QVLNQIKRRF RDETFTRQYI ADVIRDHPEL IRLLYINFAM VHYPSHEEAN QLGPTLSYQR
MQVDHPLTDE ELYTKIRRTV PNEHDQQVLT SFLVFNKHVL KTNFYQPTKV ALSFRMEPSF
LPEVEYPKTP FGLFFVIGSD FRGFHIRFKD VARGGIRIVR SRGVEQYSIN QRMLFDENYA
LASTQSLKNK DIPEGGAKGT ILPSIGANPR LCFEKYIDAI TDLLVPGHSP GIKEPIIDLY
NKPEILFFGP DEGTADMMDW AAIHARNRGV DSWKSFTTGK SAELLGGIPH DIYGMTSLSV
RQYVLGIYKA LGLKEKDVTK VQTGGPDGDL GSNEILLSSD KTIAVIDGSG VLADPAGIDR
DELVRLAKAR VMVSNFDRSK LSKDGYLILV EDQDVKLPSG EVIQDGTDFR NTAHLRFKSD
LFVPCGGRPE AVNIANVSQL FDLDGKPHFK YVVEGANLFI TREARLYLEK RGVILFKDAS
ANKGGVTSSS LEVLAGLSLN DKEYADLMIF QDGKASEFYQ SYVKDIQAKI IENAANEFSC
IWKEYNRLKG AKPRSVISDE LSSHLTDLQE ELENSDLFDD KPSRLGVMRR AIPDTLVNKI
GVDTILGRLP VAYQKALFSS WVASHFIYQF GVNGSAVDFF HFARDLAHRG
//
