ID Q0B893_BURCM Unreviewed; 1613 AA.
AC Q0B893;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Glutamate dehydrogenase (NAD) {ECO:0000313|EMBL:ABI89630.1};
DE EC=1.4.1.2 {ECO:0000313|EMBL:ABI89630.1};
GN OrderedLocusNames=Bamb_4077 {ECO:0000313|EMBL:ABI89630.1};
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI89630.1, ECO:0000313|Proteomes:UP000000662};
RN [1] {ECO:0000313|Proteomes:UP000000662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000441; ABI89630.1; -; Genomic_DNA.
DR RefSeq; WP_011659072.1; NZ_CP009799.1.
DR GeneID; 69546798; -.
DR KEGG; bam:Bamb_4077; -.
DR PATRIC; fig|339670.21.peg.4364; -.
DR eggNOG; COG2902; Bacteria.
DR Proteomes; UP000000662; Chromosome 2.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR048381; GDH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028971; NAD-GDH_cat.
DR InterPro; IPR049062; NAD_Glu_DH_ACT2.
DR InterPro; IPR049064; NAD_Glu_DH_ACT3.
DR InterPro; IPR007780; NAD_Glu_DH_bac.
DR InterPro; IPR049059; NAD_Glu_DH_HM1.
DR InterPro; IPR049058; NAD_Glu_DH_HM2.
DR InterPro; IPR049056; NAD_Glu_DH_HM3.
DR InterPro; IPR024727; NAD_Glu_DH_N_ACT1.
DR PANTHER; PTHR43403; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43403:SF1; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF05088; Bac_GDH_CD; 1.
DR Pfam; PF21075; GDH_ACT1; 1.
DR Pfam; PF21076; GDH_ACT2; 1.
DR Pfam; PF21077; GDH_ACT3; 1.
DR Pfam; PF21074; GDH_C; 1.
DR Pfam; PF21073; GDH_HM1; 1.
DR Pfam; PF21079; GDH_HM2; 1.
DR Pfam; PF21078; GDH_HM3; 1.
DR PIRSF; PIRSF036761; GDH_Mll4104; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABI89630.1}.
FT DOMAIN 35..180
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 407..496
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 551..630
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 728..1222
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1267..1607
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1613 AA; 179239 MW; 9709FE09A786B4F3 CRC64;
MEAKNEEVVA HLLSDVVEFA RGRLPEATFR IVEPFLRHYY DFVDADDLQD RSIADLYGAA
MAHWQTAQKF VPGSERLRVY NPIVEQHGWH SDHTVIEIVN DDMPFLVDSV TMAVNRLGLA
LHSALHPVFR IWRGGNGGIE RVDAGGATAP DGQSQLASFI HFEVDRCGDA ALLDTLRDDI
ARVLGDVRAS VEDWPKIVDI ARATIKDMKA RESTAEDIEA RAFLEWMAAD HFTFLGQRDY
SLVSDGSGFG LRGVEGSGFG LLRESLRPSG APDVTPLPPA AAEIITGPWP IFLTKANSRA
TVHRPGYLDY VGVKLVGADG KVTGERRFIG LYTSTAYMVS SAEIPIVRRK CANIVRRAGF
LPKGHLGKSL VTVLETYPRD ELFQADEDQL YDIALGILRL QEHQRTRLFV RRDRFDRFVS
CLAFVPRDKY NTDLRRRIAK LLVDAYNGVN VEFTPLLSES AIARIHFVVH AEPGTMPDVD
TRELEARLVQ VARRWQDDLA DALLDAFGEE QGNRLLQRYA ESFPAGYRDD YPARTAVRDI
ELIERVKESG QLAMNLYRPI EAGPRAFRFK VYRAGDPIAL SRSLPMLEHL GVRVDEERPY
RIQTQDAAPA WVHDFGLELA DDTEFDIERV KGLFEDAFDR IWSGRIENDD FNRLVLRAHL
SAREVTILRA YAKYLRQVGS TFSDAYIERA LTGNPVIARQ LVELFLLRFD PAIGGTRDVQ
AEHLLKAIET ALDQVPNLDE DRILRQFLGV INATERTNYF LLDANGEAKP YLSFKFNPAK
VPGLPEPKPM FEIWVYSPRV EGVHLRGGRV ARGGLRWSDR REDFRTEVLG LMKAQMVKNV
VIVPVGSKGG FVVKNPPPPS DREAWMREGI ACYQTFLRGL LDLTDNLAGN TIVPPPDVVR
HDPDDPYLVV AADKGTATFS DYANAISHEY GFWLDDAFAS GGSVGYDHKK MAITARGAWE
SVKRHFREMG VDTQTTDFTV VGVGDMSGDV FGNGMLLSPH IRLVAAFDHR HVFLDPNPDP
ATSFAERERM FALERSSWAD YDTSVISQGG GVYARTAKTI PLSPAVQAAL GIDAQALPPT
ELIRAILQAP VDLLYNGGIG TYVKAAHESH QQVGDRANDA VRVNGADLRC KVVGEGGNLG
CTQFGRIEFA QRGGRINTDA IDNSAGVDCS DHEVNIKILL GLVVSDGEMT EKQRNALLAE
MTDEVGLLVL RDNYYQTQAL SIAGRYSVEL LDAEARLMRW LERAGRLNRV IEFLPTDDEI
AERQTAKQGL TSPERAVLLA YSKMWLYDAL LDSDVPEDPL VAAMLVDYFP TPLQQRFNEP
MQRHPLRREI LATHLTNALV NRVGCAFVHR LMEETDAKPG DIVRACIMAR DVFDLDAVWR
DIDALDNRVA DDVQARMFVD VARLLERAAL WFLRQLQSGA VANGGVAGLI ARCRDAVQRL
APQLPSLLPT SDLEALSERQ RVLVDAGVDS ALAGRVANGD ISAALLDIAE VAATCDRSLE
LVAGVYFSLG TLLNYRWIGE RAATLPAPTH WDMLARAAAL AEIARLKRTL ATSALAESAD
STAPETIVHA WRERREAALE RYEHLLADLR ASGGASLAVL LVIVREMAVL ERA
//
