ID A0A0F2MNY9_SPOSC Unreviewed; 1075 AA.
AC A0A0F2MNY9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-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=SPSK_05871 {ECO:0000313|EMBL:KJR89901.1};
OS Sporothrix schenckii 1099-18.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR89901.1, ECO:0000313|Proteomes:UP000033710};
RN [1] {ECO:0000313|EMBL:KJR89901.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR89901.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT "Comparative genomics of the major fungal agents of human and animal
RT Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL BMC Genomics 15:943-943(2014).
RN [2] {ECO:0000313|EMBL:KJR89901.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR89901.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25480940;
RA Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA de Camargo Z.P., Felipe M.S.;
RT "Asexual propagation of a virulent clone complex in a human and feline
RT outbreak of sporotrichosis.";
RL Eukaryot. Cell 14:158-169(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR89901.1}.
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DR EMBL; AXCR01000001; KJR89901.1; -; Genomic_DNA.
DR RefSeq; XP_016592577.1; XM_016732580.1.
DR AlphaFoldDB; A0A0F2MNY9; -.
DR GeneID; 27667857; -.
DR KEGG; ssck:SPSK_05871; -.
DR VEuPathDB; FungiDB:SPSK_05871; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000033710; 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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRNR:PIRNR000184};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184}.
FT DOMAIN 720..984
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 53..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 120694 MW; E84311E7F987FF42 CRC64;
MPEDHRTLTL DTTDLPTRFP EYVDFFPPER EKMASANSTP PLLANKLVGK VREAADRHPS
PQPSHISSSL SRASGNGHRI LRSATVGYVA PEFKGRSQQM KEVGDTIRNA GWIPDSLVDK
QITWFYNELG IDDVYFQLER VDVIANHITS LYAARVAANS REDKREEIRL DMEAYDHAIY
IDTSEPGKSA ISGPRYETRL ESKYLDGSDL SKRFRVETFR SPGVLGDAST PRASLRCYFV
YQCQFVDPAA DPTESRLEVI SDRMFLAKAT KNTKQIYQEI IELAVSRTGP VIEVFDIEDS
QEKRLVVAFR SRTARGMFSA LSDLYHYYGV TSSRKYVEQF SNGITVMSIY LRPAANLDRG
FPPLEQSIHQ ITKEISLLYC VPYNKLHNLF ASGELSLQEA IYGHCVWVFV QHFLNRLGSE
YASLSDALDV KNNAHMLLLS KLKRRLRTET FTPDYILEIV SSYPNLVRAL YASFASVHLA
VGPGFERRSI APTPTVKVLS DADLRAKITK EVSNEHEEMV MTAFRVFNNA VLKTNYFTPT
KVALSFRLDP SFLPEFEYPR RLYGMFLVIS AESRGFHLRF RDIARGGIRI VKSRSKEAYG
INARNLFDEN YGLASTQQRK NKDIPEGGSK GVILLDPKQQ DKAREAFEKY IDSILDLLLP
AETPGIKNPI VDLYGKEEIL FMGPDENTAD LVDWATKHAF DRGAPFWKSF FTGKSPTLGG
IPHDEYGMTT LSVREYVQGI YRKLQLDPSH VQKMQTGGPD GDLGSNEILL SNEKYTSVID
GSGVLVDPNG IDKGELIRLA KSRVMVSQFD LAKLSSDGYR VLCDDSNVTL PTGEVVANGT
AFRNTYHLRD TGMTDMFVPC GGRPESIDLV SVNKIIKDGK SIIPYIVEGA NLFITQDAKG
RLESAGCILI KDASANKGGV TSSSLEVLAS LSFDDAGFRQ HMCHDDKGVA PEFYKAYVKE
VQNKIRENAR LEFEAIWREH EETGVSRSVL SDKLSVAITT LDEELQKSDL WADEKIRRHV
LGDALPKLLI DQIGLDTIIQ RVPDAYLRAI FGSFLASRFV YEFGSSPSQF AFFDL
//
