ID A0A1B8TZS5_9FLAO Unreviewed; 398 AA.
AC A0A1B8TZS5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=LPB3_04545 {ECO:0000313|EMBL:OBY65052.1};
OS Polaribacter vadi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1774273 {ECO:0000313|EMBL:OBY65052.1, ECO:0000313|Proteomes:UP000092584};
RN [1] {ECO:0000313|Proteomes:UP000092584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0003 {ECO:0000313|Proteomes:UP000092584};
RA Shin S.-K., Yi H., Kim E.;
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:OBY65052.1}.
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DR EMBL; LSFM01000019; OBY65052.1; -; Genomic_DNA.
DR RefSeq; WP_065318425.1; NZ_LSFM01000019.1.
DR AlphaFoldDB; A0A1B8TZS5; -.
DR STRING; 1774273.LPB03_00565; -.
DR KEGG; pob:LPB03_00565; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000092584; 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}.
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; 43476 MW; 1DE3CF84BCF27A20 CRC64;
MSQFSPFSKE ELLPQAEMLE IQKRKGELFI GLPKETYIGE KRVCLTPDAV TALCAHGHRI
VVETGAGDGA NYTDKEYSEA GAKISYNTEE AFKCNIVLKV APPTEEEIAY LNPETILISS
LQLKTQNKKY FDCLAKKKIT AVAFDYIKDE HNSYPVVKSL SEIAGTASIL IAGELMSGTN
KGNGLLFGNI GGVPPTSVVI FGAGTVGEYA ARTALGLGAR VKVFDNSISK LRNLQHCLPA
PIYTSTLQPK SITKALMRCD VAIGAIRGKN RSPVVVTETM LESMKEGAVI VDVSIDRGGC
FESSNVTSHN SPTFVKHGVI HYCVPNIPAR YSRTASVSIS NIFTPYLLDI AEEGGFENAA
RFDKSLRNGM YFYHGILTNR TVAEWFDLPF RDINLLIL
//
