ID A0A1T4PY92_9FIRM Unreviewed; 289 AA.
AC A0A1T4PY92;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
DE Flags: Fragment;
GN ORFNames=SAMN02745118_02337 {ECO:0000313|EMBL:SJZ95928.1};
OS Selenihalanaerobacter shriftii.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Selenihalanaerobacter.
OX NCBI_TaxID=142842 {ECO:0000313|EMBL:SJZ95928.1, ECO:0000313|Proteomes:UP000190625};
RN [1] {ECO:0000313|Proteomes:UP000190625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-73 {ECO:0000313|Proteomes:UP000190625};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005206}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; FUWM01000022; SJZ95928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4PY92; -.
DR STRING; 142842.SAMN02745118_02337; -.
DR OrthoDB; 9804592at2; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000190625; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
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 NCBIfam; TIGR00518; alaDH; 1.
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:UP000190625}.
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..288
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT NON_TER 289
FT /evidence="ECO:0000313|EMBL:SJZ95928.1"
SQ SEQUENCE 289 AA; 30921 MW; D8AD8396CA83660C CRC64;
MIIGVPAEIK NNENRIAITP AGVETLTNEG HEVVIEENGG VGSGISDKDY KQAGAKMLAT
PKEVFDAADM IMKVKEPLPE EYDLFKEGQI LYTYLHLAAE EELTDALMEK NVVSIAYETV
ELEDGSLPLL TPMSEVAGRL ATQEGARFLE KPQGGRGVLL GGVPGVTSAK VIVIGGGIVG
INSAKMAKGL GADVTIMDID AQQMRYLDDI FHGDVKTRMS NKYNIYDEVT KADLVIGGVL
IPGAKAPHLV TEDMIKDMKE GAVIADVAID QGGCVETTYP TTHDDPVFT
//
