ID A0A140L9G3_9CLOT Unreviewed; 374 AA.
AC A0A140L9G3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN Name=ald2 {ECO:0000313|EMBL:KXG77188.1};
GN ORFNames=AN619_07180 {ECO:0000313|EMBL:KXG77188.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG77188.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG77188.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG77188.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-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:KXG77188.1}.
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DR EMBL; LOEE01000019; KXG77188.1; -; Genomic_DNA.
DR RefSeq; WP_068555093.1; NZ_LOEE01000019.1.
DR AlphaFoldDB; A0A140L9G3; -.
DR STRING; 520762.AN619_07180; -.
DR PATRIC; fig|520762.4.peg.800; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000070456; 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 ECO:0000313|EMBL:KXG77188.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070456}.
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..297
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 374 AA; 41349 MW; DAC7EBF1B4AF852C CRC64;
MKIGVPKETA NREYRVGMTH LGVKQAVSAG NEVYVSRGAG IPSGITDAMY EEAGAVLVED
VRKVYEFADL IVKVKPPIDI ELAWLQRKQV IFSYVLPERN KELCYAFIQK EITAFGYESV
EDQEGRRPLL IPMSEIAGKM AVMMGSRFFH TIHGGKGLML GCMPGISPVE VAILGAGAAA
EGAAFIAAGI GCNVTILNRS MHRLRGMEQR LGRKATYLIL TEENLVKVLK TTDMIINTID
QMGEKDTHLI PRDMLKEMKE GTIIFDVACD TNGTIETSRP TTHDDPIYVV DGIIHCAIPN
LPGIVPRTAT MVLTEATLPY IMKLAEHGYK KAVLNHSSLR KGMCFYEGWL LHKKAAENFG
LGYKPFESCF YPCK
//
