ID A0A2H9LBU4_9ARCH Unreviewed; 367 AA.
AC A0A2H9LBU4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN Name=ald {ECO:0000313|EMBL:PIU21447.1};
GN ORFNames=COT15_02370 {ECO:0000313|EMBL:PIU21447.1};
OS Candidatus Diapherotrites archaeon CG08_land_8_20_14_0_20_34_12.
OC Archaea; Candidatus Diapherotrites.
OX NCBI_TaxID=1974404 {ECO:0000313|EMBL:PIU21447.1, ECO:0000313|Proteomes:UP000229798};
RN [1] {ECO:0000313|EMBL:PIU21447.1, ECO:0000313|Proteomes:UP000229798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG08_land_8_20_14_0_20_34_12 {ECO:0000313|EMBL:PIU21447.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) 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:PIU21447.1}.
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DR EMBL; PEXL01000025; PIU21447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9LBU4; -.
DR Proteomes; UP000229798; 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 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.
PE 3: Inferred from homology;
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 367 AA; 39858 MW; 33D60F5B90FA1A0B CRC64;
MIVGTIKEIK NNENRVGLSP MGAKELVNNK HTVLVERGAG LGSGFKDEEY ASAGAKIVDS
PKEICEKSDM VIKVKEPLPQ EYDYFREDQI LFTYLHFASG KQLTDEMLKR KICCIAYETV
EKDGKLPLLK PMSEVAGQMA IIMGAYYLAK PFQGRGMLLS PVENTKPSKT VIIGGGVVGE
NALMNANGLR GEVVLFELSD KRIAELKKKY PKARFEKSDK AKIEKEILDA DLVVGAVLVE
GAKAPKVISK DMVMKMQDGS VIVDVAIDQG GCVETSHATS HADPVFKVGG VTHYCVANMP
GAYPRTSTIA LTTATLPYAV ELANKGLKAL KDDDGFMRGL NIYKGKITHK GVADAFGLPF
VEPKTLV
//
