ID A0A0S9DDQ8_9MICC Unreviewed; 1609 AA.
AC A0A0S9DDQ8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KQO04028.1};
GN ORFNames=ASF21_07520 {ECO:0000313|EMBL:KQO04028.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO04028.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
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:KQO04028.1}.
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DR EMBL; LMLU01000001; KQO04028.1; -; Genomic_DNA.
DR RefSeq; WP_055768742.1; NZ_LMLU01000001.1.
DR STRING; 1736303.ASF21_07520; -.
DR Proteomes; UP000053418; 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;
FT DOMAIN 20..173
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 405..494
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 554..622
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 726..1219
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1266..1605
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1609 AA; 178884 MW; EF9E94FFC182E2C6 CRC64;
MSSGSRTTDQ SSSDTSGEEF VEHYFEHLAD EDAAGYAPSD LRQRALAHRD LAQTREPGAA
AIGIMDQGTS SVVLIVTDDM PFLVDSVTAE LVRQNAAIHL VVHPTFLAVR EDRSQALTGL
RRVPSTAGAS SGDTAALPNI GELVGLEGRT THIESWMSVE VTRLADAAAK ELIIDGLHRV
LGDVRSAVED WPAMRSAVRS IEASLDSITG AADIPDLRQA QELLQWLDSG NFTFLGYKEY
DLVTDDDGDD ALRVREGSGL GLLRLGSAGG HLQQLTAAGR AKARERRALV ITKANSRSTV
HRAAYLDYIG IKSFDAQGNV SGERRFIGLF ATSAYTGSVR NVPLVRDKVS EVLRRCGFPS
DSHSGKDLLS ILETYPRDEL FQIGVTDLVT TALGILRLQE RRRTRLFLRP DVYGRFMSAL
VYLPRDRYTT SVRLRIEGEL RAALDADSID FEARMSESAL ARLFFRIRLQ RGAEIPEIDA
AQLEERLVRA ARSWSEGIVE VAQERFDQDS AQSLATYWAE SFPPSYRVDY EVEDALEDIA
RFERLAESGA GVPQLHVYVP EHDGPEDARL KLYLTEAKSL TQILPYFHNL GLEVLDERPF
EITRADGRSF FLYDLGLRYP AGISALGTAS LLQDAFSAAV SGSSESDAFD RLVLSEELGW
RQVVILRSYA KYMRQMGNTN SYGFVADTLL RNPVVTRALV ALFTARFDPD LEGDRDAAST
AARAALDEGL EGVPTLDADR VLRTFANLIE ATLRTNYFQD KRYVSLKFDT ARIDGAPFPR
PKFEIWVYSP QVEGVHLRFG KVARGGLRWS DRREDFRTEV LGLVKAQTVK NAVIVPTGAK
GGFFAKQLPD PSVDRQAWLA EGQASYRTFI RGLLDITDNV ITNGTTETVV PPSRVVRHDD
DDTYLVVAAD KGTASFSDIA NELSAEYDFW LGDAFASGGS VGYDHKAMGI TARGAWESVK
RHFSELDVDT QTDDFTVVGV GDMSGDVFGN GMLLSEHIRL LAAFDHRHIF LDPDPDAAAS
FAERRRLFEL PRSSWEDYDS SLISEGGGVF PRQAKSVPVS PQVRHALGLD DGVTRISPPE
LLKAILRAPA DLLYNGGIGT YVKASDETHA EVGDRANDAI RVNGDELRAR VVGEGGNLGM
TQRGRIEAAL SGVILNTDAI DNSAGVDCSD HEVNIKIFVD RMVRAGRLQP EERAGFLHSM
TDEVARLVLQ DNIDQNVLLL NDRQRVVEWS PSYERMMDWL EQKADLDRDL EALPTTAVLR
RRIDAGQGLT SPELSVLAAY AKIELTKVLS ASTLADDPYF SETLRRYFPR QLVERFDDLL
DTHPLRRQII STVIANDIIN LGGITFAFRV MEETSVPEPV IARAFVALRE IYSFDETVDA
LAALPADFPT EHWTTVHLDL RRLLDRAVRW FVNHVEQGTP VQADIDAFKP LIAPFMARLS
GYLRGGDLER ARVGVETATA WNLPEELGRH WAEQFESFAL LDIAYSTRRV DEPVENIAQV
YYAVYDRFEV DNLLERITKL PRSDRWQALA RAALRDDLYS TVADIAVAVM RASQDMRRRD
AADRLQAWQE QNADQLQRAS NMFAEVNRLE QDDISSLSVA LRLLRSIVR
//
