ID   A0A0N1BW47_9PROT        Unreviewed;      1614 AA.
AC   A0A0N1BW47;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:KPF88043.1};
GN   ORFNames=IP70_00730 {ECO:0000313|EMBL:KPF88043.1};
OS   alpha proteobacterium AAP38.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF88043.1, ECO:0000313|Proteomes:UP000037884};
RN   [1] {ECO:0000313|EMBL:KPF88043.1, ECO:0000313|Proteomes:UP000037884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP38 {ECO:0000313|EMBL:KPF88043.1,
RC   ECO:0000313|Proteomes:UP000037884};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF88043.1}.
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DR   EMBL; LJHR01000003; KPF88043.1; -; Genomic_DNA.
DR   STRING; 1523418.IP70_00730; -.
DR   PATRIC; fig|1523418.3.peg.2077; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000037884; 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   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}.
FT   DOMAIN          35..177
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          408..495
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          552..632
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          734..1230
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1276..1609
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1614 AA;  179090 MW;  083789A92654A143 CRC64;
     MAFKLEQRKS ELLDQVVAKL RSRLSKEKAG LAEAFVRAFY RNVSPDDMLR STADELYGAA
     IAIMQFGGTR KPGDALVRVL NPRVDSDGWH AHHTVVEIVN DDMPFLVDSV SAELNRRGLT
     VHLVVHPVIK VSRDGDGRLT AIWQNGEAPA DAIAESVMHI EVDQITGNDE LDAIRASIAA
     VLADVRAAVT DFHAMRARLT ETIAGQYGPV AAEEREEGLA FLRWMDEDHF IFLGIREYRL
     GKDNGEETLD IQTGAGLGLL RDDEVSVFDG LRYFSTLPPE VKAFVRHPRF MMVTKANKDS
     TVHRRAPLDA VMVKLFNEAG EEVGERLFVG LFTSTAYNRS SRDIPFLRQK VNRVIARSGF
     DGRGHDGKAL VHILETYPRD ELFQIGDDEL FDIAMGVLHL QERQRVALFV RKDPFERFVS
     ALIHVPRDRY DTDLRKRLQA LIEKAYDGTS TQVNVSLSES VLARVHLIVQ TTPGKVPDVD
     VAELESQLIE ASRGWRDRFT QALVEEKGEA AGLALARRYN ATLPASYQEA YTPDEAVVDI
     ARIEQIIANG GIALNLHRPV EADAHQLFFK VYQTGGPVEL SKVLPMLEHL GLRILAEGGP
     FEVELPGDTP NVFMQDFDMR TADGRAVELD RVKAAFEDAF LRVWTGEAQS DGFNRLVLLS
     GMDWREVTIF RAYAKYLKQA KFDFSQEYIE NTLSTHSRIA RLLLDLFRFS HDPAILAKLG
     RDEVDTKRKG LILEIDHALD AVTNLDEDRI LRRMLNIIRT TLRTNFFQKG ADGKAKSYIS
     FKLDSGSIDD LPLPRPWREI WVYSPRVEAI HLRGGKVARG GIRWSDRKED FRTEILGLIK
     AQIVKNAVIV PVGSKGGFIV KNPVPASAGR EAVMAEVIEC YKTMMRGLLD ITDNLKNGVV
     IPPEDVVRLD SDDPYLVVAA DKGTATFSDI ANGVSREYGF WLDDAFASGG SAGYDHKGMG
     ITARGAWEAV KRHFRELGKD IQNEDFTTVG VGDMSGDVFG NGMLLSKHIR LIAAFDHRHI
     FVDPNPDAAS SWAERKRLFD LPRSSWADYD TTKLSPGGAI FDRGAKSLTL SPEIRQVLEI
     QADRVTPTEL MRAVLRAKVE LLWLGGIGTY VKSSDETNAD AGDKANDPIR LNGRELRAKV
     VGEGANLGFT QRGRIEAAQA GVSINTDAID NSAGVDTSDH EVNIKILLRD VMDGGGMTRE
     QRDVLLAQMT DEVADLVLAD NYKQTQALTI AQAISVETLE DQARFARTME KAGKLSRAIE
     FLPDDEEIAA RVNAKRGLTR PETAVLLAYA KIDLYDQLLA SDLPEDKSVE RDLMRYFPKP
     LQEKFPDALG RHQLRREIIC TAVTNGMVNR VGPTFTWEMV EQTGRREGDV ARAYLIVRDA
     FGLRRLWDAV EALDTKVPAA VQTAMMLYTG RLMRRAVPWV LAHGSYPLDI AAEVARLAPV
     VEELTGHLPD ILSPSALKWL AETAGNWSKD GVPGDLARRV SALPLLAAST DIAEIAVEAN
     RDPSDVANLY FDLGDRLGLE YLRARTAEVK AENHWQRQAV AASLDDLFNL QARLTARVLV
     QVQGGGDLFE AWAAHRTGPL ERINSLLADL RGVAALDIAM LAVAGRQLRG LLAG
//