ID A0A173KYY2_9SPHN Unreviewed; 549 AA.
AC A0A173KYY2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate dehydrogenase (NAD(P)(+)) {ECO:0000313|EMBL:ANI79358.1};
DE EC=1.4.1.3 {ECO:0000313|EMBL:ANI79358.1};
GN Name=gdhA {ECO:0000313|EMBL:ANI79358.1};
GN ORFNames=EP837_02964 {ECO:0000313|EMBL:ANI79358.1};
OS Sphingobium sp. EP60837.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1855519 {ECO:0000313|EMBL:ANI79358.1, ECO:0000313|Proteomes:UP000078304};
RN [1] {ECO:0000313|EMBL:ANI79358.1, ECO:0000313|Proteomes:UP000078304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EP60837 {ECO:0000313|EMBL:ANI79358.1,
RC ECO:0000313|Proteomes:UP000078304};
RA Lee C.-M., Yoon S.-H., Kim B.-Y.;
RT "Complete genome sequence of a organophosphorus pesticides.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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DR EMBL; CP015987; ANI79358.1; -; Genomic_DNA.
DR RefSeq; WP_066530159.1; NZ_CP015987.1.
DR AlphaFoldDB; A0A173KYY2; -.
DR STRING; 1855519.EP837_02964; -.
DR KEGG; sphb:EP837_02964; -.
DR PATRIC; fig|1855519.3.peg.3048; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000078304; Chromosome 2.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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 Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ANI79358.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000078304}.
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 549 AA; 59902 MW; EB424649C2C13605 CRC64;
MANQRITVLL VEDNPVYSRL IQKLLAKSEH QHFEVAVAST LESAIERLAV GGIDVVLLDL
MLPDSAALDT FYRLRAHDMH TPIIVQSAMD DVGLASKAVE GGAEDYLLKD GISSASLTRS
IHYAIERTHA RGAEWSSSML HLAQQQFLKA AYITGLDPNI RQRLLFPERT QICALPFKRD
GTDQVETVFA YRVQHVLTMG PTKGGLRYHP DVSLGEVAAL SMWMTWKCAL AKLPFGGAKG
GVRVDPTALS KDELERLTRR YTSEFIGMIG PEKDIPAPDM GTDAQVMAWI MDTYSEHVGY
SVPSVVTGKP VVLGGSLGRN EATGRGLAYL VSETCRQIGL DLNRATAVVQ GFGNVGMHAA
TFLAEAGAKI IGISDVSVAL HNPGGLPIDK LKDYVRQHRQ LFGCPFGEII PSRDLLELQC
DILAPCALQN QITAENSSRI NCKILAEGAN GPTTLEADDM LDARGIIVLP DILTNAGGVV
VSYFEWVQGL QNLTWPLEEI NNRMREILTD ALSRTQRRAQ AEKVDLRTAA MIEALSRVGA
ANHLRGLFP
//
