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Database: UniProt
Entry: A0A0Q6PS47_9MICO
LinkDB: A0A0Q6PS47_9MICO
Original site: A0A0Q6PS47_9MICO 
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
//
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