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Database: UniProt/TrEMBL
Entry: E6RRS3_PSEU9
LinkDB: E6RRS3_PSEU9
Original site: E6RRS3_PSEU9 
ID   E6RRS3_PSEU9            Unreviewed;       336 AA.
AC   E6RRS3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   07-JUN-2017, entry version 44.
DE   SubName: Full=Alcohol dehydrogenase, propanol-preferring {ECO:0000313|EMBL:ADT70627.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:ADT70627.1};
GN   Name=adhP {ECO:0000313|EMBL:ADT70627.1};
GN   OrderedLocusNames=PSM_B0592 {ECO:0000313|EMBL:ADT70627.1};
OS   Pseudoalteromonas sp. (strain SM9913).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=234831 {ECO:0000313|EMBL:ADT70627.1, ECO:0000313|Proteomes:UP000007933};
RN   [1] {ECO:0000313|EMBL:ADT70627.1, ECO:0000313|Proteomes:UP000007933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM9913 {ECO:0000313|Proteomes:UP000007933};
RX   PubMed=20703316; DOI=10.1038/ismej.2010.103;
RA   Qin Q.L., Li Y., Zhang Y.J., Zhou Z.M., Zhang W.X., Chen X.L.,
RA   Zhang X.Y., Zhou B.C., Wang L., Zhang Y.Z.;
RT   "Comparative genomics reveals a deep-sea sediment-adapted life style
RT   of Pseudoalteromonas sp. SM9913.";
RL   ISME J. 5:274-284(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP001797; ADT70627.1; -; Genomic_DNA.
DR   RefSeq; WP_013463315.1; NC_014800.1.
DR   STRING; 234831.PSM_B0592; -.
DR   EnsemblBacteria; ADT70627; ADT70627; PSM_B0592.
DR   KEGG; psm:PSM_B0592; -.
DR   eggNOG; ENOG4105DQ4; Bacteria.
DR   eggNOG; COG1064; LUCA.
DR   HOGENOM; HOG000294685; -.
DR   KO; K13953; -.
DR   OMA; YKGLKMT; -.
DR   OrthoDB; POG091H06JQ; -.
DR   Proteomes; UP000007933; Chromosome II.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007933};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000313|EMBL:ADT70627.1};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN       11    334       PKS_ER. {ECO:0000259|SMART:SM00829}.
SQ   SEQUENCE   336 AA;  35826 MW;  C49ED22BC3C37164 CRC64;
     MKAAINTEYK GKLEITDLPI PEVGPNDVLV KIAACGVCHT DLHACHGDWP VKPKMPLVPG
     HEGVGVIEKL GSNIKHLEVG DRVGVPWLYS ACGHCEFCLD GRETLCLSQH NTGYSIDGGY
     AEYCLAHGDY IIKIPEGLGF AEAAPLFCAG VTTYKALKVS DAKPGQWVAI VGVGGLGHLA
     VQYAKAMGFN VIAVDTGKEK MALAKELGAD ITLDFKEVVP SEAIFEQVGG AHAVVCTAVS
     KPGFEQAYKS VRRGGKCVLV GLPPEDMPLP IFDTVLNGVS VVGSIVGTRK DLQECLEFAA
     QGKVKAIIEE KKLEDINEIF DDMLKGEING RIVVTI
//
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