ID I3CBL7_9GAMM Unreviewed; 1628 AA.
AC I3CBL7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:EIJ41010.1};
GN ORFNames=BegalDRAFT_0086 {ECO:0000313|EMBL:EIJ41010.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ41010.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ41010.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ41010.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH600070; EIJ41010.1; -; Genomic_DNA.
DR RefSeq; WP_002682557.1; NZ_JH600070.1.
DR STRING; 395493.BegalDRAFT_0086; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_6; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000005744; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005744}.
FT DOMAIN 35..187
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 419..508
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 564..641
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 738..1231
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1278..1625
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1628 AA; 185596 MW; 521F586FF1E29CA3 CRC64;
MSLSLETQAT ELLQKILNDL QRNFPPYEYS QLKTFIEYFF NFLTPEDVLE RGSLIDLYGA
VVSYWQFARQ RQCDEVKIRV FNPQFEQDGW QSQHTIISIL VRDRPFLVDS VQMALNRMGI
TIYLIAHPIL CVDRDDDGNL IDVYPIAPFN SESEKEDGSA DCYESIMHIE IDRHTDVATL
AKIQQALTSV LQTLRAVVED WKPMYLQMQR IIDALAKTPP PRLDSVEVNE TKAFLEWLQA
DHFTFLGYRE YKLVKRDGED ELRVVAGSGL GILREESAVE RVSKGFHELP PALRQLASQA
QLLLLTKASS RSAIHRASYM DYVGVKQFNE QGDVIGERRF IGLYTAALYH LSTLHIPLLH
RKVRQVIEQA GFRPNSHQQR KLLTILETYP RDELLQIDIG ELLRIAMGIL RLQERQRVRL
FVRPDTYKRF YACLVFVPRD RYDSNVRERM QAVLMKVFQG NSIDFTVNLS ESVLAQVHLV
VHTSATVTPS YDVKEIEAQL VDIIRGWEDV LNTTLLDMHG EEKGTQLFRR YHAAFSSAYR
ENFRPRHAAY DIEKLERLCT DENLVMHLYK PLEALDNSLR FKLFHLDKHL PLSDVLPMLE
NMGVKVISED AYEINVSEQP IMWIQDFGLT HTQATTLDIK QLNQAFQETF KRVWSGDIEN
DGFNRLVLHP ALTWRDIVMF RAYYKYIRQA GTTFSQAYIE QTLFNNLPIT YLLSQLFHAR
CNPEQVNANQ VETLLKQLET ALDSVVSLDE DRILRKFLAV IQATLRTNFF QQDAEGEPKP
YLSFKVDPHK IPDLPEPRPL FEIFVYSPRM EGIHLRGGKV ARGGIRWSDR LEDFRTEVLG
LVKAQMVKNA IIVPVGSKGG FVCKRPPTEG GREAVQAEGI ACYKTLIRGL LDLTDNLVDN
KIVPPPNIIR HDEDDPYLVV AADKGTATFS DIANGLSKEY GFWLGDAFAS GGSAGYDHKK
MGITARGAWE SVKRHFRELG IDTQSQNFTV IGIGDMSGDV FGNGMLLSRH IRLVAAFNHQ
HIFLDPNPDP ETSFQERERL FNLPRSTWGD YNSQLISKGG GIHSRSVKSI VLTPEIRNLL
GIQTYALTPN ELIRAILCAP VDLLWNGGIG TYVKATIEHH SDVGDRTNDN LRVNGQDLRC
KVVGEGGNLG FTQRGRIEYA LAGGRLNTDA IDNSGGVDCS DHEVNIKILL NAIVNNGDMT
AKQRDQLLAE MTESVAQLVL RNNYLQTQAR SLSLLLAPSL LDVQARFIRD LESKGRLARE
LEFLPNDKVI SERRAQGIGL TAPEIAVLLA YSKITLYDAL LASDVPDDPY LHSILLNYFP
PQLPERFDKE IRQHRLKREI IATELTNMLV NRGSSVFVFL LQEGTGFPIA DIARAFRVAW
DVFDMKSLWA EIESLDGKIT TAVQYSMMLD ARKLIDRSAR WLLRNHRVPL NMQEMVSALR
PGVKRLSSIL WDIITPQERQ SLNEKHEQLI NSGVPTDTAQ RIISLEMQFS ALDIVEVTNA
TSIHFTDENA FHQRLAHVGQ LHFLLGTQLQ LHWLRDCMTA LPRDNRWSSL SRSSLRDELF
RTHRELTIAV LAQETTELLS AQALYERWKT HNELGINRCL TLLADLNHQE KIDLAMLSVA
LREIRSVL
//
