ID A0A199XVQ6_9FLAO Unreviewed; 397 AA.
AC A0A199XVQ6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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 Name=ald2_1 {ECO:0000313|EMBL:OAZ05522.1};
GN ORFNames=FLB_00520 {ECO:0000313|EMBL:OAZ05522.1};
OS Flavobacterium succinicans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=29536 {ECO:0000313|EMBL:OAZ05522.1, ECO:0000313|Proteomes:UP000093807};
RN [1] {ECO:0000313|EMBL:OAZ05522.1, ECO:0000313|Proteomes:UP000093807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD5b {ECO:0000313|EMBL:OAZ05522.1,
RC ECO:0000313|Proteomes:UP000093807};
RA Poehlein A., Daniel R., Simeonova D.D.;
RT "Draft genome sequence of Flavobacterium succinicans strain DD5b.";
RL Submitted (JUN-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:OAZ05522.1}.
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DR EMBL; JMTM01000004; OAZ05522.1; -; Genomic_DNA.
DR RefSeq; WP_064713959.1; NZ_JMTM01000004.1.
DR AlphaFoldDB; A0A199XVQ6; -.
DR PATRIC; fig|29536.5.peg.53; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000093807; 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 ECO:0000313|EMBL:OAZ05522.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093807}.
FT DOMAIN 30..163
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 175..322
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 397 AA; 43399 MW; 20674756EB80F7D0 CRC64;
MSISPFTKQQ LMPQEEKLEV ARHKSELFIG IPKETSFQEK RICLTPDAVN SLTIQGHRVM
IESGAGESSS YTDKEYSDAG AEVTKDTAKV FSCPMILKVE PPTLAEIEML NNKAIVLSAI
QLKTRQKAYF EALARKKITA LAFEYIKDED GSYPAVKSLS EIAGTASILV AAELMITTEF
GKGLLFGNIT GVPPTEVVIL GAGTVGEFAA KTAIGLGANV KVFDNSITKL RRLQNHLNQR
IFTSTIQPKA LLKALRRCDV AIGAMRGKER CPIVVTETMV ENMKKGAVIV DVSIDTGGCF
ETSEVTTHEK PTFIKSNVLH YCVPNIPSRY SKTASLSISN IITPYLLQIA EDGGLESAIR
CNKGLKNGVY LYHGILTNKA IGEWFDIQDS DINLLVF
//
