ID A0A0S9C1D8_9MICC Unreviewed; 386 AA.
AC A0A0S9C1D8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:KQN87386.1};
GN ORFNames=ASE96_12015 {ECO:0000313|EMBL:KQN87386.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN87386.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN87386.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN87386.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN87386.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN87386.1,
RC ECO:0000313|Proteomes:UP000051467};
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:KQN87386.1}.
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DR EMBL; LMLR01000012; KQN87386.1; -; Genomic_DNA.
DR RefSeq; WP_056430923.1; NZ_LMLR01000012.1.
DR AlphaFoldDB; A0A0S9C1D8; -.
DR STRING; 1736232.ASE96_12015; -.
DR OrthoDB; 5918420at2; -.
DR Proteomes; UP000051467; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047126; F:N5-(carboxyethyl)ornithine synthase activity; IEA:InterPro.
DR CDD; cd12181; ceo_syn; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR046951; CEOS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE 1; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 11..148
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 151..313
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 386 AA; 42457 MW; C43E78C55DF53ECF CRC64;
MSGTLNLLTL GVLASTRKPD ERRLPIHPLH LDRIAPELRQ QMLLEEGYGE RFGVSDAQLA
PLVARIVPRT QLLAEADVVL LPKPQPEDLA ELRDGQVLWG WPHCVQDRAI TQLAIDKKLT
LIAFEAMNHW ASDGGFGLHV FHKNNELAGY CSVLHALALT GSTGDYGRRL SAVVIGFGAT
ARGAVTALNA HGIHDVQVLT NRGVAAVGSP IHSVRIAQFD HADKAPFLSE VITERGRVPL
APFLAERDIV VNCTLQDPNA PLTYLRTEDL DAFRPGSLIV DVSCDEGMGF SWAKTTTFAE
PMFKVGDHID YYAVDHSPSY LWNSSSWEIS EALLPFLETV ITGPKAWTAN ETVRRAIEIR
DGVVLNPDVL QFQQRGAEYP HLTLTD
//
