ID A7BKE8_9GAMM Unreviewed; 1482 AA.
AC A7BKE8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Bacterial NAD-glutamate dehydrogenase {ECO:0000313|EMBL:EDN72986.1};
GN ORFNames=BGS_0027 {ECO:0000313|EMBL:EDN72986.1};
OS Beggiatoa sp. SS.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=422288 {ECO:0000313|EMBL:EDN72986.1, ECO:0000313|Proteomes:UP000003533};
RN [1] {ECO:0000313|EMBL:EDN72986.1, ECO:0000313|Proteomes:UP000003533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS {ECO:0000313|EMBL:EDN72986.1};
RA Mussmann M., Hu F.Z., Richter M., de Beer D., Preisler A., Jorgensen B.B.,
RA Huntemann M., Glockner F.O., Amann R., Koopman W.J.H., Janto B., Hogg J.,
RA Boissy R., Lasken R.S., Stoodley P., Ehrlich G.D.;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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:EDN72986.1}.
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DR EMBL; ABBY01000003; EDN72986.1; -; Genomic_DNA.
DR BioCyc; BSP422288:G10LO-17-MONOMER; -.
DR Proteomes; UP000003533; Unassembled WGS sequence.
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 SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003533}.
FT DOMAIN 2..140
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 378..467
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 523..599
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 694..1188
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1233..1470
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT COILED 126..157
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1482 AA; 169331 MW; 62FBCF98CB32E87A CRC64;
MLERGSVSNL YGTAIAYWRF ARQYTADQTK VRVYNPQFEQ DGWQSAHTIV SLIIKDMPFL
VDSIRMALNR QGLTVHLIVH PILKTHRDEQ GQLLEVLPHN NDDGQLPPEE RVRRHYESIL
HVEVDRQTEE AVLENIVREL EQVLNDLRLA VADWQKMHDK MGEVVHELET NPPPINTDEI
HEICEFLYWT QTNHFIFLGY QEYALLGEDE GLVLRRLAET GLGILRDHNP PHASRHEAEE
VSSTFAKLPL ALRKLAHQPT LLLLNKTRAR STIHRPARMD YIGIKRIDQS GKVIGERRFL
GLYTSTAYHQ RTVDTPLIRQ KVMYVVEKAG FRRNSHKSQA LFYILETYPR DELFQIEPET
LLQTARGILQ LQEQQRIRLF VRPDTYGRFF SCLVYVPRER YDTDIRKRME TVLLKAFGGT
RIEFHVWLSE SVLAQVHFIV YTPTGTCLHC DIKDIENKLI EVIREWQDVL HDALLEHNGE
EQGTRLFRRY KDAFPVSYQD YFSARHAIYD IDKIEALETN GGLGMNLYRP IEVLDNSLRF
KLFHPQSHLP LSKVLPMLEN MGVNVIQERS YEVRTSDSLA VWIQDFELLH HEKSLDIAQI
KEVFQDAFAE VWHGLMENDG FNRLVLHTQF NWREVIIFRA YWKYLRQTCS NFSQEYVEQA
LVNNPQIVSL LLDLFYARCN VAQAQPFDSL VKRIEMALDS VTSLDEDRIL RRFLGVILAT
LRTNYFQKDD KGEPKPYLSF KFDPSKVPDL PEPRPMFEIF VYSPRVEGVH LRGGKVARGG
IRWSDRLEDF RTEILGLVKA QMVKNAVIVP VGSKGGFVVK RLPTEGGRDA LQAEGIACYQ
TFIRGLLDLT DNLVEGKVVP PADVVRHDSD DPYLVVAADK GTATFSDIAN NIAKAYQFWL
GDAFASGGSS GYDHKKMAIT ARGAWESVKR HFREIGLDIQ KQHFTVIGIG DMSGDVFGNG
MLLSEHIKLV GAFNHKHIFL DPNPNTKTSF QERQRLFNLP RSSWADYDNR LISEGGGVFS
RSRKSIVLSP QVQALLNKKN QVLTPNELIQ ALLCASVNLL WNGGIGTYVK AQSEHHLEVG
DRANDGLRIN GQDLRCQVVG EGGNLGFTQL GRIEYALNGG HIHTDAIDNS GGVDCSDHEV
NIKILLDAIV ANGDLTIKQR NNLLHDMTDA VAHLVIENNY LQTQVLSITQ FLSSQLLNVY
TRLIRHLESQ DQLVRALEFL PTDKTLVERR AAQQGLTSPE LCVLLAYSKI SLYKTLLNSD
LLEEPYFQKT LEHYFPAPLP ERFAKEIAQH RLRREIIATK LTNTVVNRNG ISFVFRLNEE
SGQTAPEIVR AFFVAWEVFD MQSLWDEIEA LDIQVNAQVQ IGMMIDARKQ VERATRWLLR
HHRKPLDIAK TIDTLHPGVT HLAKNLLDFI DNVERASLET SAQNLVDAGV PLILATRVAS
LVYCLSALDI VEVANANAIT LENVATVHFL FRHPSQTTLV TR
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