ID   A0A0Q9NCH7_9MICC        Unreviewed;       403 AA.
AC   A0A0Q9NCH7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Aldehyde dismutase {ECO:0000313|EMBL:KRE71609.1};
GN   ORFNames=ASG77_11315 {ECO:0000313|EMBL:KRE71609.1};
OS   Arthrobacter sp. Soil762.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE71609.1, ECO:0000313|Proteomes:UP000051715};
RN   [1] {ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE71609.1, ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|EMBL:KRE71609.1,
RC   ECO:0000313|Proteomes:UP000051715};
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:KRE71609.1}.
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DR   EMBL; LMSG01000019; KRE71609.1; -; Genomic_DNA.
DR   RefSeq; WP_056346845.1; NZ_LMSG01000019.1.
DR   AlphaFoldDB; A0A0Q9NCH7; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000051715; 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}.
FT   DOMAIN          43..153
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          194..252
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01262"
SQ   SEQUENCE   403 AA;  41985 MW;  060EF3ACB4F78B1E CRC64;
     MTGNKAVAYK EPGKVELIDI DYPSFELKDG PGVNPANVGR TVPHGVILKT VATNICGSDQ
     HMVRGRTTAP SNLVLGHEIT GEVVEVGPGV EFIKVGDICS VPFNIACGRC RNCKERKTGI
     CLNVNPDRPG SAYGYVDMGG WVGGQANYVL VPYADWNLLK FPDKDQALEK IMDLTMLSDI
     FPTGFHGAVS AGVGVGSTVY VAGAGPVGLA AATSAHLLGA AVVIVGDLNE DRLKQARSFG
     CETIDLSKGG PAEQIEQILG VPEVDCGVDA VGFEARGHGH DAKEAPATVL NSLMEITAAG
     GALGIPGLYV TGDPGGVDEA AKKGALSLSL GTGWAKSLSF TTGQCPVMKY NRQLMMAILH
     DKVSIARNVN AKAISLEDAP KGYAEFDAGA ATKYVLNPNG YLN
//