ID A0A0S8AZ00_9BACT Unreviewed; 377 AA.
AC A0A0S8AZ00;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
DE Flags: Fragment;
GN ORFNames=AMS20_08525 {ECO:0000313|EMBL:KPK04626.1};
OS Gemmatimonas sp. SG8_28.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703357 {ECO:0000313|EMBL:KPK04626.1, ECO:0000313|Proteomes:UP000051120};
RN [1] {ECO:0000313|EMBL:KPK04626.1, ECO:0000313|Proteomes:UP000051120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_28 {ECO:0000313|EMBL:KPK04626.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK04626.1}.
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DR EMBL; LJNQ01000126; KPK04626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8AZ00; -.
DR PATRIC; fig|1703357.3.peg.3673; -.
DR Proteomes; UP000051120; 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}.
FT DOMAIN 7..141
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 153..301
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPK04626.1"
SQ SEQUENCE 377 AA; 40242 MW; A9A9628FAB8EDD3B CRC64;
GTSMIIGVPR ETHRHEHRVG LTPQAVRRFI HDGHQVVVER SAGIAARFTD REYEEAGAKI
VYSSDEAYKR ADLVCKVGVV SHDELDLLKP GLVVGAFHHL TVAPRATVNR LREMDVTAIG
YELIEDASGH RSILIPFSEM AGQMAVYLAA YYLQNEVGGR GILLGNVPGI APPTVLILGA
GTVGRTAARR AVAIGAHVIV LDASLQKLRE VSRELEGRVV TQLVSPDRLE SYTRIADVVI
GAVLIPGARA PFLVSEDMVK AMRPGSVIID LSIDQGGCVE TSRPRTPEAP TYVVHDVVHY
CVPNMTANVA RTASRALADA LKAPLAELLE KGVADALRDN PGLAAGTYLY QGHVTHGPLA
AAHDVAVSPL STLLADA
//
