ID A0A2T0MC35_9FLAO Unreviewed; 399 AA.
AC A0A2T0MC35;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=CLV81_3473 {ECO:0000313|EMBL:PRX55067.1};
OS Allomuricauda pacifica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1080225 {ECO:0000313|EMBL:PRX55067.1, ECO:0000313|Proteomes:UP000237640};
RN [1] {ECO:0000313|EMBL:PRX55067.1, ECO:0000313|Proteomes:UP000237640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25027 {ECO:0000313|EMBL:PRX55067.1,
RC ECO:0000313|Proteomes:UP000237640};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRX55067.1}.
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DR EMBL; PVYX01000002; PRX55067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0MC35; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000237640; 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; 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:UP000237640}.
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; 43781 MW; 272C99337EEC05C1 CRC64;
MNQPSSPFSK QQLLPQEETL EILKQKGELF IGLPKENQYQ EKRICLTPDA VNAITAHGHR
VLVESGAGEG ANFSDTDYTD AGAEITRDTK KVFSCPLILK VEPPTLSEMD MLNPQTIVIS
ALQIKTQSKA YFEKMAKKRL TAIAFEYIRD EDGKYPAVRS LSEIAGISSI LIASELMATT
NKGNGLMFGN ISGVPPVEVV IIGAGTVGEF ASRSALGLGA NIKVFDNSLT KLRNLQTNLN
RTVYTSTIQP KNLLKALKRC DVAIGATRGK DRSPVVVSST MVENMKKGAV IIDVSIDMGG
CFETSEVTTH DKPTIEKYDV IHYGVPNIPS RYPRTSSISI SNIFTPYLLK IGEDGGLEHS
LRFDKGLRNG LYMYHGILTN KSVGDWFGLS YNDINFLIF
//
