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Database: UniProt
Entry: A0A0F5VKM5_9ACTN
LinkDB: A0A0F5VKM5_9ACTN
Original site: A0A0F5VKM5_9ACTN 
ID   A0A0F5VKM5_9ACTN        Unreviewed;       410 AA.
AC   A0A0F5VKM5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Aldehyde dismutase {ECO:0000313|EMBL:KKD02731.1};
GN   ORFNames=TN53_38860 {ECO:0000313|EMBL:KKD02731.1};
OS   Streptomyces sp. WM6386.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD02731.1, ECO:0000313|Proteomes:UP000033641};
RN   [1] {ECO:0000313|EMBL:KKD02731.1, ECO:0000313|Proteomes:UP000033641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6386 {ECO:0000313|EMBL:KKD02731.1,
RC   ECO:0000313|Proteomes:UP000033641};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (JAN-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:KKD02731.1}.
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DR   EMBL; JXTE01000115; KKD02731.1; -; Genomic_DNA.
DR   RefSeq; WP_046263560.1; NZ_JXTE01000115.1.
DR   AlphaFoldDB; A0A0F5VKM5; -.
DR   PATRIC; fig|1415558.3.peg.845; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000033641; 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   Reference proteome {ECO:0000313|Proteomes:UP000033641};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          46..155
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          208..274
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   410 AA;  42711 MW;  F28F028C41E223A0 CRC64;
     MSATGNRAVA YLKPGAVEVR TIDYPTLELQ DGPGVAAANV GRKCRHGVIL KVLASNICGS
     DQHMVRGRTT APEGLVLGHE ITGEVVERGP DVETLDVGDI VSVPFNIACG RCRNCKERKT
     GICLNVNPAR PGAAYGYVDM GGWVGGQAEY AMVPYADFNL LKFPDRDQAR EKLLDLTMLS
     DIFPTGFHGV VSSGAGVGST VYVAGAGPVG LAAAASAQLL GAAVVIVGDL NAERLAQARS
     FGCETVDVSR GSVGEQIAQI LGEPEVDAAV DAVGFEARAH GPQAPEAPAT VLNSLMGITR
     AGGALGIPGL YVTDDPGGVD ADAKSGTLKV RLGLGWAKSH RFTTGQCPVM QYHRNLMRAI
     LHGRVHIAKA VNATVIGIED APRGYAEFDQ GASRKYVLDP HGALDGVRPV
//
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