GenomeNet

Database: UniProt
Entry: D9VVR1_9ACTN
LinkDB: D9VVR1_9ACTN
Original site: D9VVR1_9ACTN 
ID   D9VVR1_9ACTN            Unreviewed;       348 AA.
AC   D9VVR1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=alcohol dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00024074};
DE            EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074};
GN   ORFNames=SSNG_04429 {ECO:0000313|EMBL:EFL17177.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL17177.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL17177.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL17177.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00023978};
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG657750; EFL17177.1; -; Genomic_DNA.
DR   RefSeq; WP_007266106.1; NZ_GG657750.1.
DR   AlphaFoldDB; D9VVR1; -.
DR   STRING; 253839.SSNG_04429; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_2_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 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          16..343
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   348 AA;  36704 MW;  B3CD0D7121C30623 CRC64;
     MSVTQAAAYA APAPKAPLER TTVPRRPVGE HDVLIEIKFA GICHSDIHQA RDGWGEGIFP
     MVPGHEIAGV VAEVGAGVTR FAVGDRIGVG CMVDSCRECE YCLAGQEQHC VQGMTGTYNA
     VGRDGEPTYG GYSTHLVVDE NYAVRIPDGL SLDVAAPLLC AGITLYSPLR HWQAGPGKKV
     AVVGLGGLGH VGVKIAAALG AEVTVLSQSL RKKDDGLRLG AAHYYATSDE ATFEELKGRF
     DLILSTVSAP LGLDRYLSLL RVGGALVNVG APEEPVELNL FSVIGGNKTL AGSMIGGIAE
     TQEMLDFCAE HGLGADIEVI RAEDVNAAYE RVLSSDVRYR FVIDASTI
//
DBGET integrated database retrieval system