ID A0A0Q7QDI6_9ACTN Unreviewed; 382 AA.
AC A0A0Q7QDI6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:KQY55977.1};
GN ORFNames=ASD11_15970 {ECO:0000313|EMBL:KQY55977.1};
OS Aeromicrobium sp. Root495.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY55977.1, ECO:0000313|Proteomes:UP000051970};
RN [1] {ECO:0000313|EMBL:KQY55977.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY55977.1,
RC ECO:0000313|Proteomes:UP000051970};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY55977.1, ECO:0000313|Proteomes:UP000051970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root495 {ECO:0000313|EMBL:KQY55977.1,
RC ECO:0000313|Proteomes:UP000051970};
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:KQY55977.1}.
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; LMFJ01000002; KQY55977.1; -; Genomic_DNA.
DR RefSeq; WP_056289852.1; NZ_LMFJ01000002.1.
DR AlphaFoldDB; A0A0Q7QDI6; -.
DR STRING; 1736550.ASD11_15970; -.
DR OrthoDB; 5918420at2; -.
DR Proteomes; UP000051970; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051970}.
FT DOMAIN 10..147
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 150..311
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 382 AA; 41515 MW; 34EA60D42EEB270E CRC64;
MSGSSLRTLG VIGTSAKENE HRLPLHPDHL ANLDDDVRAV IRLEHGYGER FGFPDDELSG
LVAGMASREE LIAESDVVLL PKPQLADVEA MRPGATLWGW PHCVQDTALT QVAIDRELTL
VAFEVMNHWT SAGGVGLHVF HKNNELAGYS SVIHAMQLAG ITGDYGRRLS AIVIGFGATA
RGAVTALNAH GVHEVAVLTN REVAAVGSPI HSVRIRQIDP APDQTSMSVI TERGREPLAA
YLAENDIIVN CTLQDPLDPV TYLVEDDLAA FRRGSLIVDV SCDEGMGFSW ARPTGFDDPA
FTVGDHVLYY AVDHSPSYLW ASATWENSAA LLPFLRTVLS GPEACEGDET LRRATEIRGG
HVLNPAILTF QDRETEHPHR VR
//
