ID A0A0Q9MT54_9BACL Unreviewed; 404 AA.
AC A0A0Q9MT54;
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:KRE69504.1};
GN ORFNames=ASL11_13985 {ECO:0000313|EMBL:KRE69504.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE69504.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE69504.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE69504.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE69504.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE69504.1,
RC ECO:0000313|Proteomes:UP000051252};
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 ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KRE69504.1}.
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DR EMBL; LMSD01000012; KRE69504.1; -; Genomic_DNA.
DR RefSeq; WP_056615051.1; NZ_LMSD01000012.1.
DR AlphaFoldDB; A0A0Q9MT54; -.
DR STRING; 1736398.ASL11_13985; -.
DR OrthoDB; 9777057at2; -.
DR Proteomes; UP000051252; 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
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; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 44..154
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 206..273
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 404 AA; 42746 MW; F47A177CAC87B83C CRC64;
MAGNKAVVYS KPGSVEIRDT DYPELVLKDG PGVNPLNIGR KCEHGVILKV VTTNICGSDQ
HMVRGRTTAP SGLILGHEIT GEVIEVGRDV EFIKKGDLVS VPFNIACGRC RSCRERNTNV
CLNVNPDRPG SAYGYVDMGG WVGGQSEYVM VPYADFQLLK FPDKEKAMEK ILDLTMLSDI
FPTGYHGAVS AGVRPGSTVY VAGAGPVGLA AAHSAQLLGA AVVIVGDLNA ERLAQAKSFG
CETVNLRENA DLAGQIDQIL GSPEVDSAID CVGFEAHGHG KAHGEAPATV LNSIMEVTRA
GGSLGIPGLY VTGDPGAVDE DSKIGTLKIR FGLGWAKSHT FVTGQTPVMK YNRDLMMAIL
SGKAQIAKAV NATLISLAEA PQAYQEFDRG VSRKFVIDPH GLVK
//
