ID A0A0S9DZM0_9MICO Unreviewed; 388 AA.
AC A0A0S9DZM0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:KQO11341.1};
GN ORFNames=ASF06_01360 {ECO:0000313|EMBL:KQO11341.1};
OS Agreia sp. Leaf244.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agreia.
OX NCBI_TaxID=1736305 {ECO:0000313|EMBL:KQO11341.1, ECO:0000313|Proteomes:UP000051484};
RN [1] {ECO:0000313|EMBL:KQO11341.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11341.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO11341.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11341.1};
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:KQO11341.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLX01000001; KQO11341.1; -; Genomic_DNA.
DR RefSeq; WP_055942399.1; NZ_LMLX01000001.1.
DR AlphaFoldDB; A0A0S9DZM0; -.
DR STRING; 1736305.ASF06_01360; -.
DR OrthoDB; 5918420at2; -.
DR Proteomes; UP000051484; 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 14..151
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 160..316
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 388 AA; 42728 MW; 20873A6EDF2B526F CRC64;
MSETTSAPAL LRLGVMATSR KADERRLPIH PAHLERIDED LRANMILERG YGLRFGIHDS
ELEPLVAAMA TRDEIIATAD VVLLPKPQAS DLEDLRDGQV LWGWPHCVQD REITQLAIDK
RLTLIAWEAM NHWQSDGGFG LHVFHKNNEL AGYCSVIHSL QLCGSTGDYG RRLTAVVIGF
GATARGAVTA LNAHGIHDVR VLTNRGIAAV GSPIPSVDII QFEHNDSAPF ESTVNTDDGP
VLLAPFLAEN DIVVNCTLQD PNAPLTYLRT EDLDASRPGS LIVDVSVDEG MGFEWARATT
FADPMFTVGE STNYYAVDHS PSLLWNSTTW EISEALMPFL RIVMEGAASW AESDTIRRAI
EIEGGEVRNP AILEFQKRST EYPYTPVQ
//
