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Benzene 1,2-dioxygenase subunit alpha (EC 1.14.12.3) (Benzene 1,2-dioxygenase P1 subunit) (Toluene 2,3-dioxygenase subunit alpha) (EC 1.14.12.11)

 BNZA_PSEP1              Reviewed;         450 AA.
A5W4F2; P08084; P13450;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 1.
07-JUN-2017, entry version 68.
RecName: Full=Benzene 1,2-dioxygenase subunit alpha;
EC=1.14.12.3;
AltName: Full=Benzene 1,2-dioxygenase P1 subunit;
AltName: Full=Toluene 2,3-dioxygenase subunit alpha;
EC=1.14.12.11;
Name=bnzA; Synonyms=todC1; OrderedLocusNames=Pput_2881;
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=351746;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
PubMed=2670929;
Zylstra G.J., Gibson D.T.;
"Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of
the todC1C2BADE genes and their expression in Escherichia coli.";
J. Biol. Chem. 264:14940-14946(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Parales R.,
Richardson P.;
"Complete sequence of Pseudomonas putida F1.";
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes both the oxidation of benzene and toluene.
-!- CATALYTIC ACTIVITY: Benzene + NADH + O(2) = cis-cyclohexa-3,5-
diene-1,2-diol + NAD(+).
-!- CATALYTIC ACTIVITY: Toluene + NADH + O(2) = (1S,2R)-3-
methylcyclohexa-3,5-diene-1,2-diol + NAD(+).
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00628};
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
Note=Binds 1 Fe cation per subunit. {ECO:0000250};
-!- PATHWAY: Aromatic compound metabolism; benzene degradation;
catechol from benzene: step 1/2.
-!- PATHWAY: Xenobiotic degradation; toluene degradation.
-!- PATHWAY: Xenobiotic degradation; xylene degradation.
-!- SUBUNIT: This dioxygenase system consists of four proteins: the
two subunits of the hydroxylase component (BnzA and BnzB), a
ferredoxin (BnzC) and a ferredoxin reductase (BnzD).
-!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
dioxygenase alpha subunit family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04996; AAA26005.1; -; Genomic_DNA.
EMBL; CP000712; ABQ79012.1; -; Genomic_DNA.
PIR; A36516; A36516.
RefSeq; WP_012052601.1; NC_009512.1.
PDB; 3EN1; X-ray; 3.20 A; A=1-450.
PDB; 3EQQ; X-ray; 3.20 A; A=1-450.
PDBsum; 3EN1; -.
PDBsum; 3EQQ; -.
ProteinModelPortal; A5W4F2; -.
SMR; A5W4F2; -.
STRING; 351746.Pput_2881; -.
EnsemblBacteria; ABQ79012; ABQ79012; Pput_2881.
KEGG; ppf:Pput_2881; -.
eggNOG; ENOG4105FUY; Bacteria.
eggNOG; COG4638; LUCA.
HOGENOM; HOG000105925; -.
KO; K03268; -.
OMA; GEYCEDF; -.
UniPathway; UPA00228; -.
UniPathway; UPA00272; UER00391.
UniPathway; UPA00273; -.
EvolutionaryTrace; A5W4F2; -.
Proteomes; UP000006553; Chromosome.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0018619; F:benzene 1,2-dioxygenase activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0018624; F:toluene dioxygenase activity; IEA:UniProtKB-EC.
GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0042184; P:xylene catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 2.102.10.10; -; 1.
InterPro; IPR017941; Rieske_2Fe-2S.
InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
InterPro; IPR001663; Rng_hydr_dOase-A.
Pfam; PF00355; Rieske; 1.
Pfam; PF00848; Ring_hydroxyl_A; 1.
PRINTS; PR00090; RNGDIOXGNASE.
SUPFAM; SSF50022; SSF50022; 1.
PROSITE; PS51296; RIESKE; 1.
PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism;
Complete proteome; Dioxygenase; Direct protein sequencing; Iron;
Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
CHAIN 1 450 Benzene 1,2-dioxygenase subunit alpha.
/FTId=PRO_0000314465.
DOMAIN 54 163 Rieske. {ECO:0000255|PROSITE-
ProRule:PRU00628}.
METAL 96 96 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 98 98 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 116 116 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 119 119 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 222 222 Iron. {ECO:0000250}.
METAL 228 228 Iron. {ECO:0000250}.
HELIX 17 22 {ECO:0000244|PDB:3EN1}.
TURN 26 29 {ECO:0000244|PDB:3EN1}.
HELIX 33 36 {ECO:0000244|PDB:3EN1}.
HELIX 39 48 {ECO:0000244|PDB:3EN1}.
HELIX 50 52 {ECO:0000244|PDB:3EN1}.
STRAND 55 59 {ECO:0000244|PDB:3EN1}.
HELIX 60 62 {ECO:0000244|PDB:3EN1}.
STRAND 68 74 {ECO:0000244|PDB:3EN1}.
STRAND 77 83 {ECO:0000244|PDB:3EN1}.
STRAND 89 95 {ECO:0000244|PDB:3EN1}.
TURN 97 99 {ECO:0000244|PDB:3EN1}.
STRAND 106 110 {ECO:0000244|PDB:3EN1}.
STRAND 112 115 {ECO:0000244|PDB:3EN1}.
TURN 117 119 {ECO:0000244|PDB:3EN1}.
STRAND 122 124 {ECO:0000244|PDB:3EN1}.
STRAND 129 131 {ECO:0000244|PDB:3EN1}.
HELIX 135 138 {ECO:0000244|PDB:3EN1}.
TURN 144 147 {ECO:0000244|PDB:3EN1}.
STRAND 153 157 {ECO:0000244|PDB:3EN1}.
STRAND 160 164 {ECO:0000244|PDB:3EN1}.
HELIX 172 176 {ECO:0000244|PDB:3EN1}.
HELIX 177 179 {ECO:0000244|PDB:3EN1}.
HELIX 180 187 {ECO:0000244|PDB:3EN1}.
STRAND 188 190 {ECO:0000244|PDB:3EQQ}.
STRAND 194 205 {ECO:0000244|PDB:3EN1}.
HELIX 209 218 {ECO:0000244|PDB:3EN1}.
HELIX 220 223 {ECO:0000244|PDB:3EN1}.
TURN 224 228 {ECO:0000244|PDB:3EN1}.
HELIX 229 234 {ECO:0000244|PDB:3EN1}.
STRAND 251 255 {ECO:0000244|PDB:3EN1}.
STRAND 257 260 {ECO:0000244|PDB:3EN1}.
STRAND 262 268 {ECO:0000244|PDB:3EN1}.
HELIX 271 286 {ECO:0000244|PDB:3EN1}.
HELIX 289 298 {ECO:0000244|PDB:3EN1}.
HELIX 301 305 {ECO:0000244|PDB:3EN1}.
STRAND 311 314 {ECO:0000244|PDB:3EN1}.
TURN 315 317 {ECO:0000244|PDB:3EN1}.
STRAND 318 320 {ECO:0000244|PDB:3EN1}.
TURN 322 324 {ECO:0000244|PDB:3EN1}.
STRAND 326 332 {ECO:0000244|PDB:3EN1}.
STRAND 334 336 {ECO:0000244|PDB:3EQQ}.
STRAND 338 347 {ECO:0000244|PDB:3EN1}.
HELIX 352 365 {ECO:0000244|PDB:3EN1}.
STRAND 366 369 {ECO:0000244|PDB:3EQQ}.
HELIX 373 386 {ECO:0000244|PDB:3EN1}.
HELIX 391 393 {ECO:0000244|PDB:3EN1}.
TURN 401 404 {ECO:0000244|PDB:3EN1}.
STRAND 406 408 {ECO:0000244|PDB:3EN1}.
STRAND 411 413 {ECO:0000244|PDB:3EN1}.
STRAND 415 419 {ECO:0000244|PDB:3EN1}.
HELIX 425 438 {ECO:0000244|PDB:3EN1}.
SEQUENCE 450 AA; 50944 MW; 038C80F197F3485D CRC64;
MNQTDTSPIR LRRSWNTSEI EALFDEHAGR IDPRIYTDED LYQLELERVF ARSWLLLGHE
TQIRKPGDYI TTYMGEDPVV VVRQKDASIA VFLNQCRHRG MRICRADAGN AKAFTCSYHG
WAYDTAGNLV NVPYEAESFA CLNKKEWSPL KARVETYKGL IFANWDENAV DLDTYLGEAK
FYMDHMLDRT EAGTEAIPGV QKWVIPCNWK FAAEQFCSDM YHAGTTSHLS GILAGLPEDL
EMADLAPPTV GKQYRASWGG HGSGFYVGDP NLMLAIMGPK VTSYWTEGPA SEKAAERLGS
VERGSKLMVE HMTVFPTCSF LPGINTVRTW HPRGPNEVEV WAFTVVDADA PDDIKEEFRR
QTLRTFSAGG VFEQDDGENW VEIQHILRGH KARSRPFNAE MSMDQTVDND PVYPGRISNN
VYSEEAARGL YAHWLRMMTS PDWDALKATR


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