ID A0A0K9YJ35_9BACL Unreviewed; 404 AA.
AC A0A0K9YJ35;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aldehyde dismutase {ECO:0000313|EMBL:KNB68679.1};
GN ORFNames=ADS79_32440 {ECO:0000313|EMBL:KNB68679.1};
OS Brevibacillus reuszeri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54915 {ECO:0000313|EMBL:KNB68679.1, ECO:0000313|Proteomes:UP000036834};
RN [1] {ECO:0000313|Proteomes:UP000036834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9887 {ECO:0000313|Proteomes:UP000036834};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-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:KNB68679.1}.
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DR EMBL; LGIQ01000017; KNB68679.1; -; Genomic_DNA.
DR RefSeq; WP_049742612.1; NZ_LGIQ01000017.1.
DR AlphaFoldDB; A0A0K9YJ35; -.
DR STRING; 54915.ADS79_32440; -.
DR PATRIC; fig|54915.3.peg.594; -.
DR OrthoDB; 9777057at2; -.
DR Proteomes; UP000036834; 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; 42559 MW; 42227C62AA538EAC CRC64;
MAGNKAVVYK GTGRVGVEDI GYPDLVLRDG PGVNPLNVGR KCEHGVILKV VTTNICGSDQ
HMVRGRTTAP EGLVLGHEIT GEVIEVGRDV EFMKKGDLVS VPFNIACGRC RSCREQKTHV
CLNVNPDRPG SAYGYVDMGG WVGGQSEYVM VPYADFQLLK FPDKDKAMEK ILDLTMLSDI
FPTGFHGAVS AGVKPGSTVY IAGAGPVGLA AAHSAQLLGA SVVIVGDLNP ERLAQARSFG
CETVDLSKHD NLGELIEHIL GEPVVDCAVD CVGFEAHGHG PNHSEAPATV LNSIMTVTRV
GGGLGIPGLY VTGDPGGIDA DAQEGTLKIR FGLGWAKAHT FVTGQTPVMK YNHSLMMSIL
SGRAQIAKAV NATLISIDDA PKGYSEFDSG AAKKFVIDPH GSVR
//
