ID T2IPP1_CROWT Unreviewed; 430 AA.
AC T2IPP1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=CWATWH0005_3683 {ECO:0000313|EMBL:CCQ54889.1};
OS Crocosphaera watsonii WH 0005.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=423472 {ECO:0000313|EMBL:CCQ54889.1, ECO:0000313|Proteomes:UP000017981};
RN [1] {ECO:0000313|EMBL:CCQ54889.1, ECO:0000313|Proteomes:UP000017981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ54889.1,
RC ECO:0000313|Proteomes:UP000017981};
RA Bench S.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCQ54889.1, ECO:0000313|Proteomes:UP000017981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ54889.1,
RC ECO:0000313|Proteomes:UP000017981};
RA Bench S.R., Heller P., Frank I., Arciniega M., Shilova I.N., Zehr J.P.;
RT "Whole genome comparison of six Crocosphaera watsonii strains with
RT differing phenotypes.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:CCQ54889.1}.
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DR EMBL; CAQL01000248; CCQ54889.1; -; Genomic_DNA.
DR RefSeq; WP_021832578.1; NZ_CAQL01000248.1.
DR AlphaFoldDB; T2IPP1; -.
DR Proteomes; UP000017981; Unassembled WGS sequence.
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; cd01076; NAD_bind_1_Glu_DH; 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; IPR014362; Glu_DH.
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 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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 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 180..419
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 143
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 430 AA; 47437 MW; DA8D2A81FC06EFC8 CRC64;
MNGLLADAST RLEKALRYTR ISEDAIERLK YPKTSLSVSI PVRMDDGSLR IFQGYRVRYD
DTRGPGKGGV RYHPNVTMDE VQSLAFWMTF KCALLNLPFG GAKGGITLNP KELSKQELER
LSRGYIEAIA DFIGPDIDIL APDVYTNQMI MGWMMDQYNI IQRKISPGVV TGKPQTMGGS
QGRDTATGTG AYYVIQTILP KFELIPEKTT VAVQGFGKAG AVVAELLGKV GYKVVAVSDS
KGGIYAEQGL DIVSIRNYKE EHQGIAAIYC QDTVCNIGEH QSITNEELLG LDVDVLIPAA
LENQITEENA DNVRAKFIFE VANGPINSAA DTILDEKGIY VFPDILVNAG GVTVSYFEWV
QNRSGLYWTK TEVNQRMRDK MMSEAQEVWS IAQQNGVSMR TAAYIHALNR LGDALDAKGT
RDYYLNGSSH
//
