DHE4_CORGL
ID DHE4_CORGL Reviewed; 447 AA.
AC P31026;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=NADP-specific glutamate dehydrogenase;
DE Short=NADP-GDH;
DE EC=1.4.1.4;
GN Name=gdh; OrderedLocusNames=Cgl2079, cg2280;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=1552846; DOI=10.1111/j.1365-2958.1992.tb01474.x;
RA Boermann E.R., Eikmanns B.J., Sahm H.;
RT "Molecular analysis of the Corynebacterium glutamicum gdh gene encoding
RT glutamate dehydrogenase.";
RL Mol. Microbiol. 6:317-326(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Guyonvarch A., David F., Leblon G.;
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000250}.
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=1.4.1.4;
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X59404; CAA42048.2; -; Genomic_DNA.
DR EMBL; X72855; CAA51376.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99472.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20415.1; -; Genomic_DNA.
DR PIR; S32227; S32227.
DR RefSeq; NP_601279.1; NC_003450.3.
DR RefSeq; WP_003856385.1; NC_003450.3.
DR PDB; 5IJZ; X-ray; 2.29 A; A/B/C/D/E/F/G/H/I/J/K/L=1-447.
DR PDBsum; 5IJZ; -.
DR AlphaFoldDB; P31026; -.
DR SMR; P31026; -.
DR STRING; 196627.cg2280; -.
DR KEGG; cgb:cg2280; -.
DR KEGG; cgl:Cgl2079; -.
DR PATRIC; fig|196627.13.peg.2015; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_2_1_11; -.
DR OMA; PCFAAFP; -.
DR BRENDA; 1.4.1.4; 960.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0006537; P:glutamate biosynthetic process; ISS:UniProtKB.
DR CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..447
FT /note="NADP-specific glutamate dehydrogenase"
FT /id="PRO_0000182768"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 168
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 37
FT /note="I -> L (in Ref. 1; CAA42048)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..410
FT /note="ANAGGVATSALEMQQNASRDSWSFEYTDERLQVIMKNIFK -> TPEAVEVF
FT RERDIRFGPGKAVNVGGVATSALEMQQNASRE (in Ref. 1; CAA42048)"
FT /evidence="ECO:0000305"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:5IJZ"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 22..41
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 58..68
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 74..85
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5IJZ"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5IJZ"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:5IJZ"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 211..226
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 352..360
FT /evidence="ECO:0007829|PDB:5IJZ"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 374..388
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 394..418
FT /evidence="ECO:0007829|PDB:5IJZ"
FT HELIX 425..444
FT /evidence="ECO:0007829|PDB:5IJZ"
SQ SEQUENCE 447 AA; 48988 MW; 0338926EA7080E35 CRC64;
MTVDEQVSNY YDMLLKRNAG EPEFHQAVAE VLESLKIVLE KDPHYADYGL IQRLCEPERQ
LIFRVPWVDD QGQVHVNRGF RVQFNSALGP YKGGLRFHPS VNLGIVKFLG FEQIFKNSLT
GLPIGGGKGG SDFDPKGKSD LEIMRFCQSF MTELHRHIGE YRDVPAGDIG VGGREIGYLF
GHYRRMANQH ESGVLTGKGL TWGGSLVRTE ATGYGCVYFV SEMIKAKGES ISGQKIIVSG
SGNVATYAIE KAQELGATVI GFSDSSGWVH TPNGVDVAKL REIKEVRRAR VSVYADEVEG
ATYHTDGSIW DLKCDIALPC ATQNELNGEN AKTLADNGCR FVAEGANMPS TPEAVEVFRE
RDIRFGPGKA ANAGGVATSA LEMQQNASRD SWSFEYTDER LQVIMKNIFK TCAETAAEYG
HENDYVVGAN IAGFKKVADA MLAQGVI
