ID A0A0M2LM21_9SPHN Unreviewed; 1539 AA.
AC A0A0M2LM21;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KKI18590.1};
GN ORFNames=XM50_12485 {ECO:0000313|EMBL:KKI18590.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI18590.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI18590.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI18590.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-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:KKI18590.1}.
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DR EMBL; LAZX01000093; KKI18590.1; -; Genomic_DNA.
DR RefSeq; WP_046409891.1; NZ_LAZX01000093.1.
DR STRING; 1642949.XM50_12485; -.
DR PATRIC; fig|1642949.3.peg.1658; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000033997; 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}.
FT DOMAIN 14..144
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 360..448
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 505..573
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 669..1160
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1205..1527
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1539 AA; 165564 MW; 30D269449955659D CRC64;
MSKASMKALT QALAERLTKG ALPGELDGFG PDERMEAAAF LAATAQTRAA GTAAVTLEQL
PGDGPQRRMR LAIVNDDMPF LVDSIAGMIG AHGLAIDRIL HPVVPVRRDA DGALESVDEA
GNRESMIYIE TERADARERR ELVDDLTAAL ADVRVAVADW RRMQATLAAD AASIEDVGGD
AEGAALIRWF LDRHFTLLGH ERWLADGSSD GEPLGISRHE HEPPLLAERS RRLAMDYFNS
GKSAPLLLKS SLLSPVHRRV PLDLVVVPIC RGATVAGLSI HAGLWTSAAL NAPPRSVPVL
RQRLADLEAK LGFDPLGHTG KALTHALATL PHDLVTAVSA ESVEELALAA MGLADRPRPK
LVLVRSALGR HLFAFAWVPR DDLSTARRVA IGDMLAEAAN GSILNWSIAL EDGRVALIRY
TIDLRQSGVV PDVAPLDARL EKMVRGWERD VEAALAERIT PSRAARLAIR WAGAFPPNYR
NLSTAEEAAE DVLRVSDLAD ENDRAVHIYP TVAGDDHRLK IYKSHGALAL SEAVPVLENF
GYRVIGELPT RLRDDSDSFV HDFMVQPQGD VANIDRVVLE EAITAVLKGV AENDAFNRLM
LVAGLTPSAV LLYRAWFRYL RQAGMTYGLS TVADALGRAP VLAKALIDRF TLAHDPAATG
DVEAIDAEIA AGLDTIVAID DDRILRAFKA VIAATLRTNA FAPAAAEALA FKLDSSRIPG
LPAPLPWREV WVYSPRVEGI HLRSGPVARG GLRWSDRRDD FRTEILGLMK AQRVKNAVIV
PSGAKGGFYP KQLPSPAVDR DAWLAEGTES YRIFIRTLLS ITDNVVAGKV VHPDGVRVHD
GEDPYFVVAA DKGTATFSDV ANAIALERGF WLGDAFASGG SHGYDHKAMG ITARGAWVSV
QRHFAERGVD VQREPIRVVG CGDMSGDVFG NGMLLSKTLK IVAAFDHRHI FLDPDPDPAA
SWTERARLFA LPRSSWEDYD KGLISAGGGV FSRTAKTIRL TPEVKAALDI AVDEIEPTAL
ISAILKAPVD LIWFGGIGTY VKAASENNAT VGDPANDRLR VDAEDLRAIA VGEGANLGVT
QAARIAFAAK GGRINTDFID NSAGVDCSDN EVNIKIALNR EMAEGRLAFD DRNTLLEAMT
DDVAHLVLED NRLQTLALSI AERGGVRAVP SYIRAIEIFE AAGRLDRRVE GLASNADLSR
RAAEGEGLTR PELAVLLSTA KLALQDAIEQ AGLGADALLE PDLRAAFPTA MQEKFGKAID
EHQLRGEIVA TKLANRIVNR IGLLNPFELA EEEGAALGDV ASMFVVVERL FDLGALWRDI
ETTAMSEDGR LALFEGVARA VRGQVADLLR VVDPGTMPGE VLKRIGGGVA KLEGQASELL
LQEARAASAR MAESLTATGA PASLVARVVR LHEMDGAIGL VDLSGKNHTD ETKLTRAYTR
LGAALGIDWA QAMAARLVPA DPWERLLVAG LARDFEQMRL DFLARDNRAD IDAVDAWLTE
NEAAVARFTA VVSRARGAAA PSAAMLAQVA SQARVLLGR
//
