ID   E3I7M0_RHOVT            Unreviewed;      1598 AA.
AC   E3I7M0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ADP69636.1};
GN   OrderedLocusNames=Rvan_0350 {ECO:0000313|EMBL:ADP69636.1};
OS   Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS   4299).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Rhodomicrobium.
OX   NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP69636.1, ECO:0000313|Proteomes:UP000001399};
RN   [1] {ECO:0000313|Proteomes:UP000001399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC   {ECO:0000313|Proteomes:UP000001399};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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DR   EMBL; CP002292; ADP69636.1; -; Genomic_DNA.
DR   RefSeq; WP_013418043.1; NC_014664.1.
DR   STRING; 648757.Rvan_0350; -.
DR   KEGG; rva:Rvan_0350; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_1_1_5; -.
DR   Proteomes; UP000001399; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000001399}.
FT   DOMAIN          30..169
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          398..486
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          543..618
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          723..1215
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1260..1593
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1598 AA;  175035 MW;  130F868151C7D07E CRC64;
     MAQKADRTGA GSSVLACPHP NATDDLASRF AAQLVAESGC SDLASGQAAA FTTLAAEAFA
     NLCRRHSPAP EISIRSHTSH EGEHIVIDIA NDDMPFLLDS VLGELRELGL IPFVVAHPIF
     EVERDGNGLL TALAPAAPEP NGHARESVIH LEIPRPGIAP SFETIDRALR RVIGDTALVV
     GDFHAMTNRL HAAIADIEQN PPPASPQTNA EGIDFLRWIA VDNFIFLGVR EFAYDAKGGE
     LIPQTKRSLG LLRDPERIVL RVEPTRVLTP ESRTYYLNAP PVVVIKANAK STVHRRVHMD
     AIAVKLHDAE RRVTGQIVFA GLFTATAYNL PVNNVPILRR TVKKVLQRSR HPAESHSGRA
     LMNVLETFPR EELFQISPER LSTISEEILK TELAPRPRVL VRRDEFRRFV TVLVYVPREK
     HNTSVRERIE AMLAESFDGR FEQTTPYYPE SAMVRLQVEI WKAGGDLLDP DERELEAKVE
     DIITTWADRF SARVLAERGG DGQALIEKYR DAFPAGYQER NDAERALKDI ERFEKLNERH
     RTGIDLYRAG DAEPDAVRAT LQQLDEPLTL SRRVPILENL GFDVISERTY LLTPKANGGA
     RRFYLHDIDL RLREGDAATF CERREALEDG FLAVWADAVP NDRFNGLILA AGLDWRQAAL
     IRAYAAYYRQ TGATYSAAYV AETLVKHGVI AADLFRLFEA MFDPAKGSDA EREAARLAIA
     ERIFAALDAI PSMDDDRILR QLASLIGATL RTNFYQRSAD GMPPEAIAFK LRSRDIEWLP
     APKPYAEIFV SSPRFEGVHL RGGSIARGGL RWSNRPQDFR TEILGLAKAQ QVKNAVIVPQ
     GAKGGFVPRA SAGANRDATY DEGVAAYEGF VSSLLSLTDN LVKGEIVPPA DTVRRDGDDP
     YLVVAADKGT ATFSDFANEI ATKRGFWLGD AFASGGSAGY DHKKMGITAR GAWEAVKRHF
     REMNVDIQTT PFTVAGVGDM SGDVFGNGML LSRKIRLVAA FDHRDIFIDP DPDTGTSFEE
     RKRLFERPRS SWQDYDRAKI SADGGVYSRK EKSIALSDAA QKLLGVGAQA TPQDVMAAIL
     RADVDLLWFG GIGTYVRAST ETDAQAGDKA NDAIRAAANE LRAKVIGEGA NLGVTQRGRI
     EFALAGGRIN TDAIDNSAGV NTSDVEVNIK IALSRAVAEG RIDTPERNAI LAAMTDDVAA
     AVLRNNYLQT LALSVAESDG LAELGFQQRL IQRLVKEGRL NRAVEALPTD AHLAERATQG
     KPLTRPELAV LLAYAKIVLE DDLVKTKALD DPFLARELPA YFPPAMRERF AAEIDAHPLR
     RAIIATSLAN DIVNRGGPTF VVRLMDETGQ SPEAVACAFA AVCAIYDLSA IHAGLDALDG
     RIDSVEQLRL YRFVRDLLRR QSGFFLRQHR FRDGLEQGIA PYAQGIAALS AEMATLLPEK
     AVARLGEAEA RLREIGLSPD FARRVAALEP LAQALDIVRV AGDMETPVED AARVVFAIRD
     AFHLDDIAAA SEALAGGDHF NRLAVDASLA GIASAQRRLA RSILAQSTRR PDFATWRARN
     EAPVSRVAEG LAEVLSGRGL TLAKLTVAVA QFRDLSAP
//