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
//