(data stored in ACNUC7421 zone)

SWISSPROT: B4SR34_STRM5

ID   B4SR34_STRM5            Unreviewed;       218 AA.
AC   B4SR34;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   SubName: Full=Cysteine dioxygenase type I {ECO:0000313|EMBL:ACF49735.1};
GN   OrderedLocusNames=Smal_0030 {ECO:0000313|EMBL:ACF49735.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49735.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49735.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49735.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF49735.1; -; Genomic_DNA.
DR   STRING; 391008.Smal_0030; -.
DR   EnsemblBacteria; ACF49735; ACF49735; Smal_0030.
DR   KEGG; smt:Smal_0030; -.
DR   eggNOG; ENOG410XWF5; LUCA.
DR   HOGENOM; HOG000057038; -.
DR   OMA; WCVEGVW; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR010300; CDO_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR12918; PTHR12918; 1.
DR   Pfam; PF05995; CDO_I; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   4: Predicted;
DR   PRODOM; B4SR34.
DR   SWISS-2DPAGE; B4SR34.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Dioxygenase {ECO:0000313|EMBL:ACF49735.1};
KW   Iron {ECO:0000256|PIRSR:PIRSR610300-51};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR610300-51};
KW   Oxidoreductase {ECO:0000313|EMBL:ACF49735.1};
KW   Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT   METAL       115    115       Iron; via tele nitrogen; catalytic.
FT                                {ECO:0000256|PIRSR:PIRSR610300-51}.
FT   METAL       117    117       Iron; via tele nitrogen; catalytic.
FT                                {ECO:0000256|PIRSR:PIRSR610300-51}.
FT   METAL       171    171       Iron; via tele nitrogen; catalytic.
FT                                {ECO:0000256|PIRSR:PIRSR610300-51}.
FT   CROSSLNK    122    188       3'-(S-cysteinyl)-tyrosine (Cys-Tyr).
FT                                {ECO:0000256|PIRSR:PIRSR610300-50}.
SQ   SEQUENCE   218 AA;  24168 MW;  624CFDD0CBC2F59C CRC64;
     MNAGATRANA NIPLTMLRYS QDMDLQTSPF PPFRGRDRLI AAVDAAMTSG DAGRITADLQ
     LALQDAIADS RIELPECVHR PVGDHYARRP LYHSREHGYS VIAMSWGPGQ GTPLHDHDAM
     WCVEGVWLGE LEITRYELLE RNGERCRFRR HAALRGGCGS AGSLIPPHEY HTLRNASDAA
     LAISVHVYEA PMERAAVFDP LGGDWYQRRI QALQADPA
//

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