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Database: UniProt
Entry: A0A0W1QQC7_9SPHN
LinkDB: A0A0W1QQC7_9SPHN
Original site: A0A0W1QQC7_9SPHN 
ID   A0A0W1QQC7_9SPHN        Unreviewed;      1540 AA.
AC   A0A0W1QQC7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KTF70731.1};
GN   ORFNames=ATB93_03130 {ECO:0000313|EMBL:KTF70731.1};
OS   Sphingomonas sp. WG.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF70731.1, ECO:0000313|Proteomes:UP000052965};
RN   [1] {ECO:0000313|EMBL:KTF70731.1, ECO:0000313|Proteomes:UP000052965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WG {ECO:0000313|EMBL:KTF70731.1,
RC   ECO:0000313|Proteomes:UP000052965};
RA   Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT   "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT   strain.";
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:KTF70731.1}.
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DR   EMBL; LNOS01000002; KTF70731.1; -; Genomic_DNA.
DR   RefSeq; WP_019367718.1; NZ_LNOS01000002.1.
DR   Proteomes; UP000052965; 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; 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; 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:UP000052965}.
FT   DOMAIN          14..146
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          356..443
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          505..566
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          668..1159
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1204..1527
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1540 AA;  168057 MW;  85D6188119203693 CRC64;
     MKNMTKEIMQ AFEERIFEGA LPGELEGLDE SERADIARFV AETAADRPPQ TVRLNLETYH
     DDNSRRMRLA VINDDMPFLV DSIAGAIAAF DLGTFRIIHP ILPVERDAKG AITAVGEKAA
     DAQAESMIYI EIERADARTR RALTSEIERV LEHVRDVVSD WRPLQQAMGL DAARVPSREG
     EALLRWFADD AMTLLGHEKW SVEGETTDQI GLARYTHDVP LLADASRNLA VDYFQMGGEI
     PLLLKSNAIS TVHRRVPLDI VATPIMRDQD VVGLSIHYGL WTSQALNTPP AMVPMLRNRL
     EMLESKFGFD PAGHTGKAMT HALTGLPHDL TTAFDLEALE SLVLTAMSVS DRPRSKLVLV
     RSPLGRHLFG FVWLPREQVA AGHRETIGNM LVEAAHAKMI NWSIALEDGV LAQLRYTLDL
     RGDTVMPDEA ELDERIARIV RGWAPAVDAC LAEIAGSGAA RLSLRLANTF PDVYRLTHTP
     EEAAQDLVRI GGLEDEHARS VRIFPVRDEA GAYRIKLYRL GGALALSDAV PAFENFGFRV
     LEEVPTELTN GAFIHDFKVE PATRSEILDR DPAVVEAAIA AVLEGRAEND LFNRLIVEAG
     LTPSAVVLLR AWFRYLRQAG MLYGMGTVVD ALRRAPIVAM ALVDRFEAAH NPARGGDAEA
     VELAEKAIDA GLAQVNAIDD DRILRLFKGV VLATLRTNAY APAGEEALAF KLDSARVPGL
     PAPLPWREIW VYSPRVEGIH LRAGPVARGG LRWSDRRDDF RTEILGLMKA QRVKNAVIVP
     TGAKGGFYPK QLPSPAVDRD AWLAEGTESY RIFIRALLSI TDNIVSGEVV HPEGVTVLDG
     QDPYFVVAAD KGTATFSDVA NKLAMERNFW LGDAFASGGS VGYDHKAMGI TAKGAWVSVR
     RHFLEMGTDI QSEPVTVAGV GDMSGDVFGN GMLLSKAIRL VAAFDHRHIF LDPDPDPSKS
     WEERARMFAL PRSSWADYNP DLISEGGGVF PRTEKSIPLS PQVKALLDLD VDSIDPNGLM
     IAILKARVGL LWFGGIGTYL KAASESNGEV GDPANDRIRI NAEQVRAQVV GEGANLGVTQ
     AARIAFARNG GRINTDFIDN SAGVDCSDNE VNIKIALNRE MVEGRLGFED RNALLASMTD
     DVAHLVLEDN RLQTLALSFM ENDGALDLPS YVRVIEILEA KGRLDRAVEG LDTNEELMRR
     AQDGRGLTRP ELAVLLASAK LALQDAIEQG DLGHDPALVG DLHAAFPKAM QERFSTAIDE
     HRLRNEIVAT KLANRVVNRL GVLHPFELAE EEGAAMRDIA AMFVAAERLF DLPSLWAEIE
     SAAISENARV ALLDQLALAV RGQIADLLRV TRPGASPAEV IDRLRSGIDV LGTKARSLLL
     DEARAHSDRI SATLEAAGAP AELADRVVRI VEMDGGVGLA ELGQRLEIDE VVLARAFTAL
     GQTLGLDWAQ GAAARITTGD VWERLLIASL ARDFQQLRLE FLGRIDGADP QAAVEAWLAE
     HQARVDQFVA VVRRARQSAA PNAAMLAQIA GQARVLLGRE
//
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