ID A0A0Q9KX42_9MICO Unreviewed; 399 AA.
AC A0A0Q9KX42;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alanine dehydrogenase {ECO:0000313|EMBL:KRE42739.1};
GN ORFNames=ASG74_10205 {ECO:0000313|EMBL:KRE42739.1};
OS Knoellia sp. Soil729.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE42739.1, ECO:0000313|Proteomes:UP000051965};
RN [1] {ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE42739.1, ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|EMBL:KRE42739.1,
RC ECO:0000313|Proteomes:UP000051965};
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:KRE42739.1}.
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DR EMBL; LMSA01000002; KRE42739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9KX42; -.
DR STRING; 1736394.ASG74_10205; -.
DR Proteomes; UP000051965; 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 15..151
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 154..317
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 379..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 43879 MW; B5D73285E7A5C724 CRC64;
MARSAETSPL LSLGVMARSR KENERRLPIH PAHLDRIDPE LRAQIFVEEG YGLPFGVPDE
TLAASLGGVR TRAELIEQCD VILQPKVQSE DLAEMRDGQV VWGWPHCVQD TPLTQEAIDR
RLTLIAFEAM NHWARDGSFL LHVFHLNNEL AGYSSVIHSL ALSGTTGTYG RKLRAVVIGF
GATARGAVTA LSAQGIDDVR VLTSRKVAAV ASPIHSVQIV HLDHDDEDPN QTRVVTNEGR
VPLATYLADN DIVVNCVLQD PTAPWTFLQE EDLGAFRPGS LIVDVSCDEG MGFSWARPTS
FEDPTFVVGT NNTTYYAVDH TPSYLWNSAT WVNSEAILPH LRTVLSGPTA WAQEPTIDRA
VEIQDGEIRN PAILSFQGRD ETYPYAQSGA REDDGSRSD
//
