ID A0A1J4UKQ0_9ARCH Unreviewed; 368 AA.
AC A0A1J4UKQ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=AUJ13_02980 {ECO:0000313|EMBL:OIO24059.1};
OS Candidatus Micrarchaeota archaeon CG1_02_49_24.
OC Archaea; Candidatus Micrarchaeota.
OX NCBI_TaxID=1805248 {ECO:0000313|EMBL:OIO24059.1, ECO:0000313|Proteomes:UP000181889};
RN [1] {ECO:0000313|EMBL:OIO24059.1, ECO:0000313|Proteomes:UP000181889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_49_24 {ECO:0000313|EMBL:OIO24059.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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}.
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:OIO24059.1}.
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DR EMBL; MNVF01000058; OIO24059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4UKQ0; -.
DR UniPathway; UPA00527; UER00585.
DR Proteomes; UP000181889; 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; IPR008142; AlaDH/PNT_CS1.
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 PIRSF; PIRSF000183; Alanine_dh; 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; PS00836; ALADH_PNT_1; 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}.
FT DOMAIN 4..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..295
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 368 AA; 39324 MW; A30DF3290A561C93 CRC64;
MIVGVPKEIK DNENRVALTP AGAMELTKRG HTVYVEANAG KGSGFPDGEY TSAGAEIIPT
AKEVFDKAEI IVKVKEPLDP EIPMLNEKKI LFTYLHLASD VEMTKKLIKS KVIGIAYETV
EKNRLLPLLA PMSEVAGRMA PIIGSYYLQK PKGGYGMLLS GAPGTEPARV VIVGGGFVGA
NAARIAYGMG ADVTILDVDE AKIRDLNNRF PYAKVLMSNE YNLRNALKGA HLLVGAVLIP
GAAAPKVVKK GMLKFMVEGA VAVDVAIDQG GVLETSHPTK HSDPVFVVDG VTHYCVTNMP
GAYPRTSTIA LTNATLPYLL KLADKGLEAL KADAGFMKGL NLYKGKITFK AVSDLFSMEY
TEPESAIG
//
