ID A0A176TFN5_9FLAO Unreviewed; 398 AA.
AC A0A176TFN5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=LPB303_03285 {ECO:0000313|EMBL:OAD46216.1};
OS Polaribacter atrinae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1333662 {ECO:0000313|EMBL:OAD46216.1, ECO:0000313|Proteomes:UP000076923};
RN [1] {ECO:0000313|EMBL:OAD46216.1, ECO:0000313|Proteomes:UP000076923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 17473 {ECO:0000313|EMBL:OAD46216.1,
RC ECO:0000313|Proteomes:UP000076923};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Polaribacter atrinae KACC17473.";
RL Submitted (FEB-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:OAD46216.1}.
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DR EMBL; LVWE01000004; OAD46216.1; -; Genomic_DNA.
DR RefSeq; WP_068448082.1; NZ_LVWE01000004.1.
DR AlphaFoldDB; A0A176TFN5; -.
DR STRING; 1333662.LPB303_03285; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000076923; 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:UP000076923}.
FT DOMAIN 31..164
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 176..323
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 398 AA; 43555 MW; 2EE41F324D40732F CRC64;
MSSFSPFSKE ELLPQEEMLE IKRQKGELFI GLPKETYLGE KRVCLTPDAV SALCAHGHRV
VIETGAGDHA NYADKEYSEA GAKISYDIEE AFKCNIVLKV APPTEKEIEY INPQTILISS
LQLKTQNKKY FECLAKKRIT AVAFDYIKDD HNTYPIVKSL SEIAGTASVL IAAELMSGIN
KGNGLLLGNI GGVPPSSVVI FGAGTVGEYA AKTAIGLGAR VKVFDNSISK LRKLQDSLSA
PIYTSTLQPK SVAKALMRAD VAIGAIRGKN RSPICATEEM IETMKEGAVI IDVSIDRGGC
FETSNVTTHK TPTFIKHGVV HYCVPNIPAR YARTASLSIS NIFTPYLLDI AEEGGFENAA
RFDKSLRNGM YFYHGILTNK TVADWFNLPF RDINLLML
//