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Database: UniProt
Entry: E3BFG3_9VIBR
LinkDB: E3BFG3_9VIBR
Original site: E3BFG3_9VIBR 
ID   E3BFG3_9VIBR            Unreviewed;      1613 AA.
AC   E3BFG3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:EFP98141.1};
GN   ORFNames=VIBC2010_10142 {ECO:0000313|EMBL:EFP98141.1};
OS   Vibrio caribbeanicus ATCC BAA-2122.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP98141.1, ECO:0000313|Proteomes:UP000002943};
RN   [1] {ECO:0000313|EMBL:EFP98141.1, ECO:0000313|Proteomes:UP000002943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP98141.1,
RC   ECO:0000313|Proteomes:UP000002943};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EFP98141.1}.
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DR   EMBL; AEIU01000022; EFP98141.1; -; Genomic_DNA.
DR   RefSeq; WP_009599650.1; NZ_AEIU01000022.1.
DR   STRING; 796620.VIBC2010_10142; -.
DR   eggNOG; COG2902; Bacteria.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000002943; 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   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:UP000002943}.
FT   DOMAIN          35..172
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          403..492
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          548..627
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          725..1219
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1265..1603
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1613 AA;  183728 MW;  E80265B65CD5640F CRC64;
     MTARETLMPV LLEKVYKLIQ DKLDLAHQPL VTQLAQHLFS NVAQDDLVER NESDLYGAVI
     SLWHHINEQK PDQISVRVFN PTVSRQGWQS THTIVEIVVP DCPFLVDSIK MALSRLDLSS
     HLMLHGPTQI GRGDKGKITG INQGEGALQS LFHIEVDRLT DKAEMTSLKE ELLSILNDTE
     LVVKDWLLMV EKLEQVTSHV ESQQGKVKTE CDRYEESIRF LRWLGDHNFT FMGYKEYDLV
     SIEGDLELRP TEDKGYGLLA KSERLRSARL SNFPYSARQE IEKSSLIVVT KGNRASRIHR
     PAYTDHIGIK KLDKNGKVIG EHRFIGLFTS AVYNQSVEGI PLIREKVERI LDYSGYREGS
     YSFRALHNIL ENYPRDELLQ AKEEELLEVG TGVVQMQDRD LLRLFVRKDP FGRFFSCMVY
     VTKDRYNTEL RRQTQSILKQ YFGCEQEVEF TTYFSESPLA RTHYIVRVDS TDIDVDAKMI
     EQNLMEASSN WDDRLSDAII ANFGESKGLP LSKAYQRAFP RSYKEDVLPG SAVADIERLE
     ELNDDNKLGM LFYRPQELAS DSKSVKLKLY HRDEPIHLSD VMPMLENLGM RVIGESPYEV
     RKSNGQVFWI LDFSMLHKSE KTVDLREARD RFQQAFASIW SGELESDGFN RLVLSASLTG
     RETSLLRAYA RYMRQVGFPF SQQYIEDTLN HYPDLAKGLV ELFTKRFDPK LKGVEKGQSD
     LIAKMMEQLD HVESLDDDRI IRRYMEMITA TLRTNYYQLD KKKHPKPWLS LKLKPSEIPE
     IPQPVPAFEI FVYAPDIEGV HLRGGKVARG GLRWSDRQED FRTEILGLVK AQQVKNTVIV
     PVGAKGGFVC KRQHTLSGRD EIFAEGQRCY KRFIRALLDV SDNIIDGEVS HPQNVVRHDE
     DDPYLVVAAD KGTATFSDLA NSVSEEYNFW LGDAFASGGS NGYDHKAMGI TAKGGWESVK
     RHFREMGINC QTTDFTAIGV GDMAGDVFGN GMLLSKHIRL QAAFNHLHIF IDPNPDSAKG
     WKERDRLFKL PRSSWEDYDK DLISKGGGIF SRRAKSIQLS PEIQKMVGTK KTSMAPNDLI
     KLILKMEVDL LWNGGIGTYV KASSETHTDV GDRANDVLRV DGKELRAKVV GEGGNLGLTQ
     LGRVEYSLNG GRVNTDFVDN VGGVDCSDNE VNIKIFLNSL VVNGDLTVKQ RNKILESMED
     EVGEIVLDDA YCQSETISVT EYKGRSLVKE QIRFIHTMEK AGHLDRALEH IPDDETLLER
     EKQGLALTRP ELSVLVAYGK MVLKEELVHE DIAKDEFHAQ QLINYFPTEL RRNYSEQMSS
     HPLRAEIIAT ALANQMVNEM GCNFVTRLQE ETGACVVDIA NAYTASREIY SLGKVFEEVR
     ALDNQASAEA QYDIFFYVRR TLRRLTRWFL QNRSGRQSVK ELIECYQANV EIIQAGLDDM
     LVPSEVEEHN DMAKAWIKNG VTTEVANYVA RLSSLYSVLD ISTVAKEKGK SIEQTAKLYY
     NLGDRLSLHW FLKQINSQGV ENNWQALARA AFREDLDWQQ RQLTGQVLNC ACDPGELHVM
     NALEQWIEIN QASLHRWENI LNEFKVGSVH EFAKFSVALR ELMLLNLNCS GNE
//
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