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Database: UniProt
Entry: A0A0Q9CXG5_9CELL
LinkDB: A0A0Q9CXG5_9CELL
Original site: A0A0Q9CXG5_9CELL 
ID   A0A0Q9CXG5_9CELL        Unreviewed;       387 AA.
AC   A0A0Q9CXG5;
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:KRD47525.1};
GN   ORFNames=ASE27_04285 {ECO:0000313|EMBL:KRD47525.1};
OS   Oerskovia sp. Root918.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Oerskovia.
OX   NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD47525.1, ECO:0000313|Proteomes:UP000051694};
RN   [1] {ECO:0000313|EMBL:KRD47525.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD47525.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD47525.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD47525.1,
RC   ECO:0000313|Proteomes:UP000051694};
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:KRD47525.1}.
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DR   EMBL; LMJG01000001; KRD47525.1; -; Genomic_DNA.
DR   RefSeq; WP_056646147.1; NZ_LMJG01000001.1.
DR   AlphaFoldDB; A0A0Q9CXG5; -.
DR   Proteomes; UP000051694; 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:UP000051694}.
FT   DOMAIN          11..148
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          151..312
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   387 AA;  42359 MW;  8D2C3C4E7CA95D5E CRC64;
     MTTASNDSIL GLLGASRKPD ERRLPLHPDH LERIAPELRA RIVVERGYGE RFGVSDEQIA
     PWVRSLGTRA EVIEAADVVL LPKPQHEDLR DLRPGQTLWG WPHCVQDRGL TQLAIDKRLT
     LVAFEAMHHW AADGGFGLHV FHKNNEMAGY CSVLHALELC GSTGDYGRRL TAVVIGFGAT
     ARGAVTALNA HGIHDVRVLT NRRVAAVAAP IHSAQIVQFD HDDGPYLSEV ITDDGRLPLA
     PFLAESDIVV NCTLQDPNAP LLYLRTSDLG AFRPGSLIVD VSCDDGMAFD WARSTTFADP
     LVTVGESINY YAVDHSPSYL WNSATWEISS AVLPFLPAVM AGPAGWDENE TVRRAIEIRD
     GVVLNPAVLE FQHREAAYPH LPVTDPA
//
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