ID A0A1Y1RGZ7_9BACT Unreviewed; 373 AA.
AC A0A1Y1RGZ7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=B6244_08070 {ECO:0000313|EMBL:OQY28200.1};
OS Candidatus Cloacimonetes bacterium 4572_55.
OC Bacteria; Candidatus Cloacimonadota.
OX NCBI_TaxID=1971726 {ECO:0000313|EMBL:OQY28200.1, ECO:0000313|Proteomes:UP000192623};
RN [1] {ECO:0000313|Proteomes:UP000192623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-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:OQY28200.1}.
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DR EMBL; NBMB01000026; OQY28200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RGZ7; -.
DR STRING; 1971726.B6244_08070; -.
DR Proteomes; UP000192623; 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; 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 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}.
FT DOMAIN 4..138
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 150..299
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 373 AA; 40217 MW; 721365A81F1CE4FF CRC64;
MIIGLVKDNR RYESRVSLTP TGVAVLVNSG HTVYVEKGAG KLSGFLSEDY LQVGARIAYS
TEEMYGRSDI VLRMSPLTVS ELEFLREGQI ICSAMHLSIA PKKVFDVLLE KKVTAIGIEL
LQHEKGYYPV LESMGQIAGR MSIQIAAQYL QSNRGGRGIL LSGVPGVPPA VIVVIGAGIV
GLNSALTALG IGAQVIVLDN DVGKLRRLET LASARATTSF SNEIAIKKSL KFADVVISSV
LLPGGERAPH VISEDMIKKM KSRSVLIDIS IDQGGCTATS RPTTLRDPVF VRHDVIHYCV
PNIPASVGRT ATHSLNNALL PFVSDIANKG IQGAVRSRIN FGKSIFTHNG YSVNEVTSKI
FDVDYTSIHD AMR
//
