ID A0A0Q6PS47_9MICO Unreviewed; 405 AA.
AC A0A0Q6PS47;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Aldehyde dismutase {ECO:0000313|EMBL:KQV04947.1};
GN ORFNames=ASC63_14050 {ECO:0000313|EMBL:KQV04947.1};
OS Leifsonia sp. Root112D2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV04947.1, ECO:0000313|Proteomes:UP000051914};
RN [1] {ECO:0000313|EMBL:KQV04947.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV04947.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV04947.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV04947.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KQV04947.1}.
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DR EMBL; LMCU01000002; KQV04947.1; -; Genomic_DNA.
DR RefSeq; WP_055815700.1; NZ_LMCU01000002.1.
DR AlphaFoldDB; A0A0Q6PS47; -.
DR STRING; 1736426.ASC63_14050; -.
DR OrthoDB; 241504at2; -.
DR Proteomes; UP000051914; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08282; PFDH_like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014184; HCHO_DH_non_GSH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02819; fdhA_non_GSH; 1.
DR PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051914}.
FT DOMAIN 44..153
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 190..251
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|Pfam:PF01262"
SQ SEQUENCE 405 AA; 42033 MW; ACB89DB26BEEC83F CRC64;
MPGNRAVAYK SPGKVEVIDI DYPTFELKDG PGVNPANVGR QVRHGAIVKT VATNICGSDQ
HMVRGRTTAP ADLVLGHEIT GEVVEVGPDV EFIKVGDLVS VPFNIACGRC KNCKERKTGV
CLNVNPDRPG SAYGYVDMGG WVGGQANYVL VPYADWNALK FPDKDQAMEK ILDLAMLSDI
FPTGYHGAVS AGVTTGSTAY VAGAGPVGLA AATSAQLLGA AVVIVGDMNA DRLAQARSFG
CETVDLSKGE PLDQIEQILG VPEVDSAVDA VGFEAKGHGA DAKEAPATVL NSLMVMTAAG
GALGIPGLYV TGDPGGVDEA AKTGSLSLNL GAGWARSLSF TTGQCPVMKY NYGLMKAILA
DRVHIAKNVN AKAISLEDAP RGYEEFDKGA ATKYVLNANG YLDAA
//