(data stored in ACNUC7421 zone)

SWISSPROT: Q82Q54_STRAW

ID   Q82Q54_STRAW            Unreviewed;       479 AA.
AC   Q82Q54;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAY-2019, entry version 123.
DE   SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:BAC68377.1};
GN   ORFNames=SAVERM_667 {ECO:0000313|EMBL:BAC68377.1};
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS   NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC68377.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC68377.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2] {ECO:0000313|EMBL:BAC68377.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
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DR   EMBL; BA000030; BAC68377.1; -; Genomic_DNA.
DR   RefSeq; WP_010982105.1; NZ_JZJK01000088.1.
DR   STRING; 227882.SAV_667; -.
DR   EnsemblBacteria; BAC68377; BAC68377; SAVERM_667.
DR   KEGG; sma:SAVERM_667; -.
DR   eggNOG; ENOG4107RVZ; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276709; -.
DR   OMA; KMARYSY; -.
DR   OrthoDB; 267896at2; -.
DR   BioCyc; SAVE227882:G1G23-751-MONOMER; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   4: Predicted;
DR   PRODOM; Q82Q54.
DR   SWISS-2DPAGE; Q82Q54.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000428};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000428}.
FT   DOMAIN        8    325       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      364    470       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     184    191       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING      54     54       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     117    117       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000350-
FT                                3}.
FT   BINDING     274    274       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     316    316       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     45     50       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   479 AA;  50823 MW;  0B7714DEF48A6632 CRC64;
     MNETARTYDV IVIGGGPVGE NVAERARAAG LSAVIVEREL LGGECSFWAC DPSKALLRPV
     VARADASRVP GLDPAVAGPL DVEAVLAHRD MMSSYWKDED QADWLNAVSV DLIRGHGRLT
     GCKEVAVQTS EGDTIALTAR HAVAVSTGTR AALPPIPGFD TVRPWTSREA TSADKVPDRL
     AVVGGGVVAV EMATAWQALG SQVTMLVLEN GLLERMEPFA GELVADGLRE AGVDIRFSTT
     VTSMAREGGE DGEVRITLSD GRELAADEIL LATGRAPQTR DVGLETVGLT PGDWLTVDDT
     FRVTGVDGGW LYAVGDVNRR ALMTHQGKYQ ARIAGTVIGA RAKGEPIDDA PWGAHVATAD
     HAAVPQVVFT TPEVASVGLT SREAEQSGRR IEVVDYDLAR VAGAHQYGDD YRGRARMLID
     TDRNTVVGVT FAGPGVGELV HSATIAVAGE VPLDRLWHAV PAFPTLGEVW LRLLETYRG
//

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