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TODB_PSEP1
ID   TODB_PSEP1              Reviewed;         107 AA.
AC   A5W4F0; P13370;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Toluene 1,2-dioxygenase system ferredoxin subunit;
GN   Name=todB; OrderedLocusNames=Pput_2879;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RX   PubMed=2670929; DOI=10.1016/s0021-9258(18)63793-7;
RA   Zylstra G.J., Gibson D.T.;
RT   "Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the
RT   todC1C2BADE genes and their expression in Escherichia coli.";
RL   J. Biol. Chem. 264:14940-14946(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein seems to be a 2Fe-2S ferredoxin.
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC       subunits of the hydroxylase component (todC1 and todC2), a ferredoxin
CC       (TodB) and a ferredoxin reductase (TodA).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       ferredoxin component family. {ECO:0000305}.
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DR   EMBL; J04996; AAA26007.1; -; Genomic_DNA.
DR   EMBL; CP000712; ABQ79010.1; -; Genomic_DNA.
DR   PIR; C36516; C36516.
DR   RefSeq; WP_012052599.1; NC_009512.1.
DR   PDB; 3DQY; X-ray; 1.20 A; A=2-107.
DR   PDB; 4EMJ; X-ray; 2.40 A; B=1-107.
DR   PDBsum; 3DQY; -.
DR   PDBsum; 4EMJ; -.
DR   AlphaFoldDB; A5W4F0; -.
DR   SMR; A5W4F0; -.
DR   STRING; 351746.Pput_2879; -.
DR   EnsemblBacteria; ABQ79010; ABQ79010; Pput_2879.
DR   KEGG; ppf:Pput_2879; -.
DR   eggNOG; COG2146; Bacteria.
DR   HOGENOM; CLU_055690_5_2_6; -.
DR   OMA; TLECWLH; -.
DR   OrthoDB; 1681886at2; -.
DR   BioCyc; MetaCyc:MON-11351; -.
DR   UniPathway; UPA00273; -.
DR   EvolutionaryTrace; A5W4F0; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism;
KW   Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2670929"
FT   CHAIN           2..107
FT                   /note="Toluene 1,2-dioxygenase system ferredoxin subunit"
FT                   /id="PRO_0000314467"
FT   DOMAIN          4..99
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         43
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         62
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         65
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          90..93
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:3DQY"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:3DQY"
SQ   SEQUENCE   107 AA;  11890 MW;  FDBFC82AD5C9C75C CRC64;
     MTWTYILRQG DLPPGEMQRY EGGPEPVMVC NVDGEFFAVQ DTCTHGDWAL SDGYLDGDIV
     ECTLHFGKFC VRTGKVKALP ACKPIKVFPI KVEGDEVHVD LDNGELK
 
 
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