ID A0A0J1D7N7_9BURK Unreviewed; 1574 AA.
AC A0A0J1D7N7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KLU35105.1};
GN ORFNames=AB595_20115 {ECO:0000313|EMBL:KLU35105.1};
OS Massilia sp. WF1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU35105.1, ECO:0000313|Proteomes:UP000036336};
RN [1] {ECO:0000313|Proteomes:UP000036336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA Lou J., Gu H., Wang H., Xu J.;
RT "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT contaminated soil.";
RL Submitted (JUN-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:KLU35105.1}.
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DR EMBL; LELH02000030; KLU35105.1; -; Genomic_DNA.
DR RefSeq; WP_047826731.1; NZ_LELH02000030.1.
DR PATRIC; fig|1406431.3.peg.3732; -.
DR Proteomes; UP000036336; 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; 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; 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:UP000036336}.
FT DOMAIN 35..167
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 392..478
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 541..602
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 707..1198
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1247..1537
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1574 AA; 171223 MW; CF416FD118CB7DA9 CRC64;
MNKDMPQDLR TRTLALVNEN KPAEQGKGQV NALIGAWLAS LDDEDLAGVS PDSLAAILQD
GFAQVAQRTG PGCQIAQMRY TDGRCGMSTA LLILNEDMSY LVDSFVMALR RQRVVASGVM
NAVLPVQRDE NGAVVDVGAA GAPLESYVLC LLGEDLPQDE LNALVERLQM VARDAAVVHR
DAVAMGDRMS AVAADAAAQG TPGGQEVAAF LEWAKNEGFE PFGYAYYFVK PGVRELERDI
PSRIGVLQDT SHPVYATSIQ NIPGDFEILS KREETLSIVK ADVAGTLHRD QPLDFIGVRA
TDAQGNTIGE HCFIGLFTRA ATSTPLARLP FARGRVAKVL GIAGVRQEGF RAEKFLEILE
SLPRTEALEA DPEWLAQVCS AVVSLYKQPR AKVFARRDVY NRHLNVLVYL PRERYSAAVV
ASLAQALKDS SGAVDVRTQT LVADGPLARV YLIAQAARYP LDLETDIQKP LLSVLDGWHD
RYTVLTEDIA DVPTRNALRK LMPTLPVNYV AATDPEVAFR DLCALLNNGK PNHVSVRIEN
DAATGASIRL YSTGSVPSLS RILPALQNAG VAIDREQAFA ITTKDGARHF VTSLIVDQES
AAKLARPGIS EVAEELFAAL FNDEAEDGRL NGLTIEGGLS TREVQLVRAY ISYWRQAGSK
FTTRYMAETL RDRAALVREL VEGFKLRFDP ALGEDERASG NAKLAALKTG LAQVNHADTE
EILAALVDLV MATVRTNYFQ GDEQNRGDKV IFKFDTSSLA LVPEPRPFRE IYVFSRRFEG
VHLRGGPVAR GGLRWSDRME DYRTEVLGLV KAQIAKNAVI VPTGSKGGFV CKQMPKDAAR
EVVAAEGEAV YRLFIASLLE LTDNRVRGEI VAPADTVRYD QDDPYLVVAA DKGTATFSDI
ANSIAVSRGF WLGDAFASGG SNGYDHKKMG ITAKGAFEAV KRHFYEMGHD MNTTPITMVG
VGDMSGDVFG NGVLLSRQLK VLAAFDHRHI FLDPNPDVAV SFTERQRMFA LPRSSWEDYD
KKLISEGGGV FPRSARHIEL TPQVRAALDI AETSLTPEEL MHRILLAPVD LFYNGGIGTY
IKASTETHAQ VKDRANDNIR VNGSELRCKV VTEGGNLGAT QAGRIEFALA GGRIFTDAID
NSAGVDCSDH EVNVKVWLDT EVNAGQLPEA DRNHLLTAMT GDIEHLVLRN NTLQTHLLVR
EAQAQSNSAV VDGYAALIAS LELEGAISRE LEQLPLDSEL ARRKALGQGL TTPELAVVIA
AVKNRFKRIL AALPLTELPW AETVLRPYFP QQLVATRDPL AHPLANTILA TMLANESVNR
CGPLMLRDLA LEHRIDDAEV VKAWGQAWSA LHLAPVFEAL DADALTVPRD VSQTVDARTR
TMLRTVTEGV LSLPLEQAGA GGMAELSQLF SEPEQLLQLN TSKSDADAHA GLPPSFAQAW
KAVDTVESLA AFLFAAVSVQ RPSGMSLAEF LQVGMVLRAA SGIDTLERGL KLPATSKSQE
QLRNYAMQAL RRTQQRMLLT VLERAKQTGD MQAAVQETTS AMGLTGFAQP TDLEQAMLNV
WSLSEGSSPE RLAA
//
