ID A0A0Q4C1E1_9SPHN Unreviewed; 1584 AA.
AC A0A0Q4C1E1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KQM19666.1};
GN ORFNames=ASE49_05535 {ECO:0000313|EMBL:KQM19666.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM19666.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM19666.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19666.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM19666.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19666.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQM19666.1}.
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DR EMBL; LMJY01000012; KQM19666.1; -; Genomic_DNA.
DR RefSeq; WP_056770748.1; NZ_LMJY01000012.1.
DR STRING; 1735670.ASE49_05535; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000050893; 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; 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; 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:UP000050893}.
FT DOMAIN 50..159
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 379..467
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 534..601
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 708..1199
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1244..1572
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1584 AA; 170806 MW; 97EE88EF29959208 CRC64;
MSEGDVDVSK KASKKRGGHP PDALHAGLCD ELRATVLPGE EADGTWIEEA ARFLLAAADQ
RAPGKTAIDV TSASEERRIL RIALINDDMP FLVDSAAAAV AQAGLVIDRL AHPVIPVRRD
GDGKLLELPA GPDGATARES MIYIETPRAD ARQRRELLRS LETTFADVRA AVADWQAMVA
AMRADADRAD GAGIGDTEGA ELLRWLADGM LTQIGHVTRH RDGTRTQPLG VCRDAPEDLL
SDQSYARAFA VFDAQLAEGA IRAPLVVKAN RMSTVHRRVP MDLFLVPVIK AGKVTALSVH
AGIWTSAALA APPSRVPRLR RHFSEMAARL ELDPVGHTGK ALAHALTSLP HDLVLGFAQE
DVERLAMMMT GLVDRPRPRL LLARSPLMRH LFAFVWLPRD LLSTQMQKRI QHMIEEAAQA
PTLDWSMQVE AGNLAMLRYT LDVREGAQEP SEDELDGALQ VILRGWTQAV EAALATTLEP
GRAAAVAARY AEAFPIGYRS EFGAAEAATD IAYLRRIAVG EGAGTAEVEA AHRDVRFHAR
EGDPENWLRL KIYQSEGGLA LSDAVPALEN FGFRVMAEVP TPLEKGALGT IHDFLVETAD
GRAPGDVLNR AAAIEDALRS VLNGSGENDA FNRLVPALGL SSTEVNWLRA WYRYLRQAGT
HFGIPTVVDA LEGAAGVTVG IVALFKALHD PAFAGDRIKA RKEAEDAIRN GLAGVSAIND
DRVLRAYRDI VLAMLRTNAF APAGEVALAF KFDSAQVPGL PKPLPWREIF IYSQRVEGIH
LRAGPVARGG LRWSDRRDDF RTEVLGLMKA QRVKNAVIVP TGAKGGFYPK QLPDPARDRA
AWAAEGQASY EVFVDTLLSI TDNIVNDKVA HPESVVVLDG EDPYFVVAAD KGTAKFSDVA
NAIAEARDFW LDDAFASGGS NGYDHKAMGI TAKGAWLSVQ RHFLELGVDV QADPVRVVGC
GDMSGDVFGN GMLLSKSLRL VAAFDHRHIF LDPTPDPKAS WEERARLFDL PVSSWNDYDK
ALISPGGGVF PRSMKSIPLS EEVRSVLGLT QAEIDPDALI TAILCAPVDL LWFGGIGTYV
KASAENNVQV GDPTNDALRV SGNELRVRVV GEGANLGVTQ AGRIEFATRG GRINTDFIDN
SAGVDCSDNE VNIKIALAAA KRAGKLTEPK RVELLRDMTD EVATLVLEDN RLQALALSIA
ERGGAQASPS HIRLIETMGD SGYLDRRTEG LPDNDVLVRR AQDGRGLTRP ELAVLLSSGK
LQMQAAIEDS TLPSDPGLTD LLLSAFPTQM QHKFAKFIKG HRLAREIIAT KLANRVINRL
GIVIPFELAE EEGTDLSQVA AAFALADRLF DLSALWERLE VAPMAETTRV ALFETVALAV
RGHMADLLRA GAGQIAPSEL ADRLQKGIAA LSTDTLDLLG ERTLAHSRKL RDGLTQMGAP
DDMAAQVANL FDLDGAVGIA SLAAETGIAP RRLVTAFTRV GAGLGLDWAQ ANAAMMSPSD
PWERLLVAGL ARDFQQMRLD FLRGLARTKA GKADPLAATE EWGRQHAAAI TAFRGIVHRA
ESAVAITPAM LAQIASQARN LLGR
//
