ID A0A1S9PK50_9SPHI Unreviewed; 408 AA.
AC A0A1S9PK50;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=BC343_20090 {ECO:0000313|EMBL:OOQ61289.1};
OS Mucilaginibacter pedocola.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1792845 {ECO:0000313|EMBL:OOQ61289.1, ECO:0000313|Proteomes:UP000189739};
RN [1] {ECO:0000313|EMBL:OOQ61289.1, ECO:0000313|Proteomes:UP000189739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBZ30 {ECO:0000313|EMBL:OOQ61289.1,
RC ECO:0000313|Proteomes:UP000189739};
RA Huang J., Tang J.;
RT "Genomic analysis of zinc-resistant bacterium Mucilaginibacter pedocola
RT TBZ30.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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:OOQ61289.1}.
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DR EMBL; MBTF01000002; OOQ61289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9PK50; -.
DR STRING; 1792845.BC343_20090; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000189739; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR CDD; cd05305; L-AlaDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008141; Ala_DH.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
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.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000189739}.
FT DOMAIN 37..170
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 182..330
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 408 AA; 44207 MW; 3CA682881F4C57B6 CRC64;
MSSGKYSGFS DVARQALMLP QESMLEVKSK KNKLYIGIPK EVSFQENRIP LTPLSVALLV
NNGHDVYLES NAGQAANFSD TNYSEQGAQI VYDTKRVYEA DIIIKVAPPT LEEIAMMKPG
QLLISALQVA TLKPECLQAM LAKKITAICF ENIEDEGGTL TVVRAMSEIV GATSILIAAE
YLSNIFGGKG LMLGGITGVP PTEIVILGAG TVGEYAARTA ISLGAEVKVF DPSIYKLRRL
QNNIGSRIFT SVVQPIVLEK AVTTCDVAIG AMRADDGRSP CLVSEATVAK MKPNSVIIDV
SIDQGGCFET SEVTNHTHPV FRKYDVIHYC VPNIASRVAR TATYALTNIF APILLDIGEQ
GGLKNVIWKK TGIRNAVYIY QGHLTNKHMG ERFNIPCKDL DLLVAANH
//
