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Database: UniProt
Entry: A0A401SPB6_CHIPU
LinkDB: A0A401SPB6_CHIPU
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ID   A0A401SPB6_CHIPU        Unreviewed;       547 AA.
AC   A0A401SPB6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Glutamate dehydrogenase 1, mitochondrial {ECO:0000256|ARBA:ARBA00040147};
DE            EC=1.4.1.3 {ECO:0000256|ARBA:ARBA00012889};
GN   ORFNames=chiPu_0010679 {ECO:0000313|EMBL:GCC32218.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC32218.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC32218.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
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=1.4.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00023525};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC         NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00023549};
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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:GCC32218.1}.
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DR   EMBL; BEZZ01000420; GCC32218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401SPB6; -.
DR   STRING; 137246.A0A401SPB6; -.
DR   OMA; MAWMYDE; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR   Gene3D; 1.10.287.140; -; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT   DOMAIN          254..543
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   547 AA;  60353 MW;  1132BEC7846E0466 CRC64;
     MYRYLGELLA RGAAASSPSA GEGGLQRICG PAALLHRRRY STEPSAAQQQ DDPNFFTMVE
     GFFDRGAKIV EDKLVEDLRT RESDEQKHNR VRGILRIIKP CNHVLSISFP IKRDNGEWEV
     IEGYRAQHSQ HRTPCKGGIR YSMDVCVDEV KALASLMTYK CAVVDVPFGG AKAGVKINPK
     NYTDSELEKI TRRFTIELAK KGFIGPGIDV PAPDMSTGER EMSWIADTFA TTMGHQDINA
     HACVTGKPIS QGGIHGRISA TGRGVFHGIE NFINEASYMS VLGMTPGFGD KTFVIQGFGN
     VGMHSMRYLH RYGAKCVGVG ELDGSIWNDD GIDPKELEDY KLAHGTIVGF PKAKPYDGNI
     LEAECDILIP AAGEKQLTKS NARKVKAKII AEGANGPTTP EADTIFMERN IMVIPDLYLN
     AGGVTVSYFE WLKNLNHVSY GRLTFKYERD SNYHLLMSVQ ESLERKFGKH GGTIPVVPTA
     EFQARIAGAS EKDIVHSGLA YTMERSAKQI MRTGMKYNLG LDLRTAAYVN AIEKVFKVYN
     EAGLTFT
//
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