(data stored in SCRATCH zone)

SWISSPROT: C5DD00_LACTC

ID   C5DD00_LACTC            Unreviewed;      1047 AA.
AC   C5DD00;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   OrderedLocusNames=KLTH0B07172g {ECO:0000313|EMBL:CAR21661.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21661.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21661.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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|PIRNR:PIRNR000184}.
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DR   EMBL; CU928166; CAR21661.1; -; Genomic_DNA.
DR   RefSeq; XP_002552099.1; XM_002552053.1.
DR   STRING; 381046.XP_002552099.1; -.
DR   EnsemblFungi; CAR21661; CAR21661; KLTH0B07172g.
DR   GeneID; 8290939; -.
DR   KEGG; lth:KLTH0B07172g; -.
DR   HOGENOM; HOG000162582; -.
DR   InParanoid; C5DD00; -.
DR   KO; K15371; -.
DR   OMA; SVDFFHF; -.
DR   OrthoDB; 90287at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
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   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028971; NAD-GDH.
DR   InterPro; IPR016210; NAD-GDH_euk.
DR   Pfam; PF05088; Bac_GDH; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   PIRSF; PIRSF000184; GDH_NAD; 1.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DD00.
DR   SWISS-2DPAGE; C5DD00.
KW   Coiled coil {ECO:0000256|SAM:Coils}; NAD {ECO:0000256|PIRNR:PIRNR000184};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN          668..939
FT                   /note="ELFV_dehydrog"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   COILED          368..388
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1047 AA;  117697 MW;  860C3CF99420356D CRC64;
     MLSSQNSKVP DISSLSISSI SDYHNFDFPG KDAQREAVLD LVDQQGFIPD DVVEHEVEWF
     YDALGIDDLF FSKESPEMIA NIIHTLYASK VESFAKLKIA GDSAASVEDG SSPSNFTVKN
     QVVTETHSVF METGNDLDKE IDSMLLDNPT QRYRLISYTA ESALKLTFVY RTVFAAEDQS
     GAELAPEQLC HGDIDSISDL TMSQVTSKEN KKLYGLIMNQ MRQREGPVIK TLHSVADQDE
     VRIVVGFKRG TTKSYYAALS SLLHYYHLKP SKIYMETFTN DVMIYSLYLK QSQQSESVLN
     SLPMSIMQIE REASLLYAIP SNFFQDLYQQ RSFSPQEAIY AHISAIFINN FINRLGDDYQ
     NLVAQISVSG ANKNNNSAQE VLASLKKKLR NETYTQQMII DVLHKYKSIV SKLYKNFAQV
     HYVSSSSSKF GKTLSYQRLS KLEPFKDDNE FELYLNKFIP NDSPDMLVLK TLNLFNKSIL
     KTNFFITRKV AISFRLNPAL IMPEVEFPET PFGIFFVVGN TFKAFHIRFR DIARGGIRIV
     CSKTQDIYEV NSKMAIDENY QLASTQQRKN KDIPEGGSKG VILLNPTLTS PEQTFVAFSQ
     YVDAIIDILI QDPLKEKYVD LLGQEEILFF GPDEGTAGFV DWATSHAKSR GCPWWKSFLT
     GKSASMGGIP HDDYGMTSLS VRAFVNGLYE TLGLQEKTIH KFQTGGPDGD LGSNEILLSS
     SNEQYVALVD GSGVLCDPSG LDMAELKRLA NERKMVTSYD KSKLKHHGFF VSVDEVDIIL
     PNGVIVANGT TFRNRFHLEI FNFVDKVDLF VPCGGRPNSI DINVLHFYVD EKTSRCKIPY
     IVEGANLFIT QPAKIALENH GCILFKDAST NKGGVTSSSM EVQASLALND ADFINKFIGK
     EPQQRTPLYA AYVEEVQDRI QKNARAEFNQ LWQLNQSTGT PISELSNVLS QTINKVNDEL
     INSNELWVND LKLRNFLLLK KIIPKLLIDV AGPTSVLENI PVSYLKALLS SYLSSTYVYS
     YGIDVNIGKF LEYIGELKRE AEDFALA
//

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