ID A0A0H1AM91_9GAMM Unreviewed; 1640 AA.
AC A0A0H1AM91;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KLI99811.1};
GN ORFNames=WQ56_11380 {ECO:0000313|EMBL:KLI99811.1};
OS Luteimonas sp. FCS-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLI99811.1, ECO:0000313|Proteomes:UP000035397};
RN [1] {ECO:0000313|EMBL:KLI99811.1, ECO:0000313|Proteomes:UP000035397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLI99811.1,
RC ECO:0000313|Proteomes:UP000035397};
RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Luteimonas oceanisediminis
RT sp. nov., a novel gammaproteobacteria isolated from a marine sediment.";
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:KLI99811.1}.
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DR EMBL; LASZ01000012; KLI99811.1; -; Genomic_DNA.
DR STRING; 1547516.WQ56_11380; -.
DR PATRIC; fig|1547516.3.peg.2397; -.
DR Proteomes; UP000035397; 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:UP000035397}.
FT DOMAIN 35..167
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 399..488
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 544..620
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 760..1255
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1300..1634
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1640 AA; 181847 MW; 442ADA4325F781F2 CRC64;
MPAPPRRVGA GLLDPIFEAV RRRAGKAAQR GADAFAQGFY RRMTEEELPL HSADGWAALA
ADLFDFAARR KPGTANVRLF NPVQGTHGWE SPHTVLQIVN DDMPFLVDSV TMALAERSVG
VHVLGHPVLH IARDRAGRLT GVGEGDAESV MHLEIDRQTP EESARIEQVV RRVLEDVRAI
VADWGPMREK MQEVAADLVL RPMPVADASR REAQEFLRWA ASDHFTFFGY REYKVRRKGG
DGVLEAVPDS GLGLLRTPAA VKSRPLSELG ADALRRAGEV DALILTKTSA RSTVHRPGYM
DYIGVLRYDA KGQVVGEQRF LGLYTSSAYT RRPWDIPLVR ERFEHVMSES GLKPTGHSGK
TLKHLLETLP RDELFQSTPD ELFRLGTGIL GLQERVRSRL FLRRDRYGRF YSVLVYIPRD
RFNTDVRHRV EDMLRETMQA DHVDAHVVLG ESPLAQLHLI VRPRAGVQGE VDQAALEQAL
QKIVRNWHDD LRDELVRRHG EGEGLRLAGR LGRGLSAAYI EFASPAVAAT DVEKLAAAQG
SGALQLSFYN QVTSPTGDTL LHFKLYRSGQ HLPLSEVLPV MENLGLRVIA ENPTRLTVDG
TALFIQDFFV ETLAANVDID ARAPAFTEAF DRVWRGDAEN DGFNRLILAA DLDWRQVAML
RGYCKYLQQV GVPFSQAYVE DTLGRYPLLA RLLVEVFEAR FDPATGRESR AQIAAGVEAL
SSQLGALSGD EATLALLQPV LDARAGDRDA QYDAARAALK GLLDRVSSLD EDRILRSYLG
VIDATLRTSY YQRTPEGAVR DTIAFKFDSA RVPELPKPRP YREIFVYGPR VEGIHLRFGP
VARGGLRWSD RREDFRTEVL GLVKAQMVKN TVIVPVGSKG GFIVKRPPAG GDRDALFAEG
VACYTLFING LLDITDNIVD GDIVPPRDVV RHDDNDPYLV VAADKGTATF SDIANGIARE
HGFWLDDAFA SGGSVGYDHK GMGITARGAW ESVKRHFRAL GRNSQTQDFT AVGVGDMSGD
VFGNGMLLSE HIRLVAAFDH RHIFIDPDPD AARSFVERQR LFALPRSSWA DYDTGLIGKG
GGVWPRSAKS IPLSKEARAA LGIDGDVTAL SPNELMSAIL RAPVDLLWNG GIGTYVKASS
ESHADVGDRA NNPLRVDGRD LRCRIVGEGG NLGMTQLGRI EAAQHGVLLN TDFIDNSAGV
DTSDHEVNIK ILLNAVVQSK KLTVPARNKL LASMTDEVAG LVLWDNYRQN QALSLMERMS
VARLGSKRHF IRTLEAQGLL DRQIEFLPSD AELSERKAKG LGLTRPELAV LLSYSKLVAF
DQMLDSDIPE DPYLSRELQR YFPAPLQKKY AAVMEQHRLK REIIATAVTN QMINRMGATF
LLRMQEDSGR SPGEVAKAFT ITRETIEARA LWNRIDALDG TVPEAVQVDA LQVIWNLQRA
FTRWLLARAG AIPDITTAVE RYHDGFHAIR NGSQIIADSQ RAEHDASLQV WRDKGVPEDL
AEQLAALPYL EAAWDIVEVA SETRRKPIDV ARVHFRLGEA LNLPWLTAQI DALEVDGRWH
AVARGVLRED LGQQHRILVG QVLAMPGDTP EEKVRTWLER DDQTLRFTLA MLAELAAQKT
LDYATVSVAV QRVSQLVQRS
//
