ID A0A0Q5UHU8_9FLAO Unreviewed; 397 AA.
AC A0A0Q5UHU8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=ASG38_15350 {ECO:0000313|EMBL:KQS45981.1};
OS Flavobacterium sp. Leaf359.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS45981.1, ECO:0000313|Proteomes:UP000051024};
RN [1] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS45981.1}.
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DR EMBL; LMPW01000015; KQS45981.1; -; Genomic_DNA.
DR RefSeq; WP_056073756.1; NZ_LMPW01000015.1.
DR AlphaFoldDB; A0A0Q5UHU8; -.
DR STRING; 1736351.ASG38_15350; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000051024; 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:UP000051024}.
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; 43442 MW; F300E39563422D08 CRC64;
MSFTPFTKQQ LIPQEEKLEV ARKKSDLFIG IPKESSFQER RICLTPDAVN TLTSHGHRIL
IEAGAGESSS YSDQEYSNAG AEITQDTKKV FNCPMVLKVE PLTLPEIEMM NSNSLVISAI
QIKTRKKEYF EALARKKITA LAFEFIKDDD GSYPAVKSLS EIAGTGSILI AAELMINNQF
GKGLLFGNIT GVPPTEVVII GAGTVAEFAA RTAIGLGASV KVFDNSITKL RRLQNNLNQR
IFTSTIQPKS LLKALRRCDV AIGAMKGKDR CPVVVSETMV EHMKKGAVIV DVSIDTGGCF
ETSEVTTHEK PTFIKNDVIH YCVPNIPSRY SKTASLSISN IITPSLLQIA EDGGIESAIR
CNKGLKNGVY FYHGILTNKT IADWFDLPGS DINLIVF
//
