ID A0A1P8RTF9_9FLAO Unreviewed; 399 AA.
AC A0A1P8RTF9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=BWZ20_01960 {ECO:0000313|EMBL:APY07141.1};
OS Winogradskyella sp. J14-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1936080 {ECO:0000313|EMBL:APY07141.1, ECO:0000313|Proteomes:UP000187462};
RN [1] {ECO:0000313|EMBL:APY07141.1, ECO:0000313|Proteomes:UP000187462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J14-2 {ECO:0000313|EMBL:APY07141.1,
RC ECO:0000313|Proteomes:UP000187462};
RA Kim J.H., Chi W.-J.;
RT "Genome sequence of Winogradskyella sp. J14-2 isolated from seawater in
RT Jeju island.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; CP019388; APY07141.1; -; Genomic_DNA.
DR RefSeq; WP_076615522.1; NZ_CP019388.1.
DR AlphaFoldDB; A0A1P8RTF9; -.
DR STRING; 1936080.BWZ20_01960; -.
DR KEGG; wij:BWZ20_01960; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000187462; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000187462}.
FT DOMAIN 32..165
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 177..324
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 399 AA; 43259 MW; 3E60DB7C7B6AFFBC CRC64;
MSKSLSPFTK AQLLPQEETL EVFKKKGELF IGIPKETHFQ ESRVCLTPDA VSALTANGHR
VLFESGAGEG ANFKDKDYSE AGAEVTKDTA KVYSCPMVLK VEPPSLDEIA LINPQTILIS
ALQIKTQSKS YFEALAKKRI TALAFEYIKD DDGAYPAVRS LSEIAGTASI LIASELLSNV
NGGNGLMMGN INGVPPTEVL ILGAGTVGEF AARSAMGLGA NIKIFDSSIT KLRCIQNNLG
RSVYTSTMQP KNLLKALKRC DVAIGAVRGT NRSPVVVTET MVEHMKPGSV IIDVSIDMGG
CFETSEVTTH DHPTFDHNGV IHYCVPNIPA RYSRTASVSI SNIFTPYLLE IGEHGGLENA
LRFDRGLKNG LYFYHGILTN KSVAEWFGLD YNDANLLIF
//
