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Database: UniProt
Entry: A0A1Y1CJI1_9BACT
LinkDB: A0A1Y1CJI1_9BACT
Original site: A0A1Y1CJI1_9BACT 
ID   A0A1Y1CJI1_9BACT        Unreviewed;       444 AA.
AC   A0A1Y1CJI1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=ALGA_2213 {ECO:0000313|EMBL:BAX80546.1};
OS   Labilibaculum antarcticum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC   Labilibaculum.
OX   NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX80546.1, ECO:0000313|Proteomes:UP000218267};
RN   [1] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:BAX80546.1, ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|EMBL:BAX80546.1,
RC   ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 39:1-2(2018).
RN   [3] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT   psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL   Antonie Van Leeuwenhoek 113:349-355(2020).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC       ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; AP018042; BAX80546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1CJI1; -.
DR   KEGG; mbas:ALGA_2213; -.
DR   OrthoDB; 9803297at2; -.
DR   Proteomes; UP000218267; Chromosome.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
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; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000185}.
FT   DOMAIN          202..442
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         209
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            166
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   444 AA;  48374 MW;  8871BAC57C84E9E9 CRC64;
     MEAKINEFME GLKAKTPGEV EFHQAVQEVV ETVWDTYDAN PKYKAAKILD KMCEPERTIM
     FRVPWINDNG EVEINRGYRV EFNSAIGPYK GGLRFHPSVT LSALKFLGFE QTFKNSLTTL
     PMGGGKGGSD FNAKGRSDNE IMRFCQSFMT ELCRHIGPNT DVPAGDIGVG GREIGYLFGQ
     YKRIRNEFVG VLTGKGLEFG GSLIRPEATG FGAVYFAQHM LAENNESLKG KTVALSGFGN
     VTWGAALKLV ELGAKVVTIS GPDGYVYDKE GLNAEKIDYL LDLRASNNDV VAPYADKFGA
     VFFPGKKPWE AKVDLAFPCA IQNELNLEDA ELLISNGCKY VVETSNMGCT ADACNYLVVN
     AVFAPGKAAN AGGVAVSGLE MSQNSMRFNW STEEVDEKLG RIMKDIHDTC VKFGTENGHI
     NYIKGANIGG FVKIAEAMLA QGCV
//
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