ID A0A0Q9QNA3_9MICC Unreviewed; 1613 AA.
AC A0A0Q9QNA3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KRF04269.1};
GN ORFNames=ASH00_14265 {ECO:0000313|EMBL:KRF04269.1};
OS Arthrobacter sp. Soil782.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736410 {ECO:0000313|EMBL:KRF04269.1, ECO:0000313|Proteomes:UP000053496};
RN [1] {ECO:0000313|EMBL:KRF04269.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04269.1,
RC ECO:0000313|Proteomes:UP000053496};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF04269.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04269.1,
RC ECO:0000313|Proteomes:UP000053496};
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:KRF04269.1}.
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DR EMBL; LMSO01000011; KRF04269.1; -; Genomic_DNA.
DR RefSeq; WP_056549744.1; NZ_LMSO01000011.1.
DR STRING; 1736410.ASH00_14265; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000053496; 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 Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 20..176
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 404..493
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 554..624
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 729..1222
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1269..1608
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT COILED 1568..1595
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1613 AA; 181575 MW; 872BB11F411130EE CRC64;
MSSGSSTTEQ SSSDTSFTEF IQHYYQHLAD DDAGTYSPDA LTKRALEHRS VAAIRSTGEA
LVGVFDQDDA SIVMIVTDDM PFLVDSVTAE LVRQHAAIRL VVHPTFVTVR HRSSHELMRL
RRVPSSAGSS SGDTAALPNL ADLVAESDVS AHVESWIAVE IGRISDEKRR AEIIEGLQRV
LTDVRAAVED WAAMRSKLRE VSSTLQQVPA DAGIPGLEQA QELLAWLDGG NFTFLGYKEY
DLETENGEDV LRVREDSGLG LLRHPIDGRP VQHLTQAGRA KAREKQPLVI TKANSRSTVH
RAAYLDYIGI KRFDSQGNVS GERRFIGLFA TSAYTGSVRS VPIVRDKVNE VLHRCGFPSD
SHSGKDLLSI LETYPRDELF QVDVDDLVTT AMGILRLQER RRTRLFLRPD TYGRFMSALV
YLPRDRYTTS VRLRIEDELR RTFKAESIDY EARMSESALA RLFFRIRLPK GAEVAHVEVA
ELEQRLVMAA RSWSEGIDEV ARTRFNRRDA DRFSRLWAEA FPAAYRVDYE VEDALEDIER
FAAYDRMDTA GPIMHVYVPS GAGEHLEEDA RLKLYLTEPK SLSQILPFLH NLGLEVLDER
PFEIERSDGR DFFLYDLGLR YPQGIDPTGT GELLEEAFAA AMANASESDS FDRLVLKENL
RWRQVAILRS YAKYMRQMGN MNSYGFISDT LLANPGVTRK LIALFEGRFD PDLSSGQREE
TTARVRRELD SDLEQVPTLD ADRVLRTFAN VIEATLRTNY FQDQHHISYK LNTAAIEGAP
HPRPKFEIWV YSPQVEGVHL RFGDIARGGL RWSDRREDFR TEILGLVKAQ TVKNAVIVPT
GAKGGFYAKQ LPDPAQDRAA WMAEGQASYR TFIRALLDIT DNLVTTEDGE RVVPPERVVR
HDGDDSYLVV AADKGTASFS DIANELSAEY GFWLGDAFAS GGSVGYDHKA MGITARGAWE
SVKRHFSEFG VDTQSEEFTV AGVGDMSGDV FGNGMLLSTH IRLVAAFDHR HIFLDPNPDA
SRSFDERKRL FELPRSSWAD YNPELISEGG GVYARHVKSI PVSVQVREAL GLDPSVTSMS
PPELLRAILS APVDLLYNGG IGTYVKASTE SHADVGDKAN DAIRVDGNQL RARVVGEGGN
LGMTQRGRIE AALKGVILNT DAIDNSAGVD CSDHEVNIKI FVDRMVRMGR LGEDERTEFL
HSMTDEVAEL VLQDNIDQNV LLLNDRQRVL EWSPSFERLM DWLESHADLN RELEALPTTA
ELRSRVESGQ GLTAPELSVL AAYAKIELTK ALTRSDLADD PWFKGTLRRY FPRQVVERFD
EELDTHPLRR EIISTVIAND MVNMGGITFV FRVMEETSVN ESVVARAFVA LREIYELDHI
VEALSELPPS FPTEHWTTVH LDVRRLLDRA VRWFVNHVGR GTTVEEDIAA FKPLLDPLRT
KLVNYVRGGD LERVRSWFQR AEEWGLPDSI AQHWAEQFES FGLLDVALIS RRVDEPVERI
AEVYYAIYDR FNVDNLLERI TSLPREDRWQ ALARAALRDD LYSTVSEMTV SVMNSSSHLG
SSDASSRLQE WENLNAEHLD RAKKMFAEVN QLERDDMASL SVALRLLRSI VRQ
//
