BNZA_PSEP1
ID BNZA_PSEP1 Reviewed; 450 AA.
AC A5W4F2; P08084; P13450;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Benzene 1,2-dioxygenase subunit alpha;
DE EC=1.14.12.3;
DE AltName: Full=Benzene 1,2-dioxygenase P1 subunit;
DE AltName: Full=Toluene 2,3-dioxygenase subunit alpha;
DE EC=1.14.12.11;
GN Name=bnzA; Synonyms=todC1; OrderedLocusNames=Pput_2881;
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 1-12.
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: Catalyzes both the oxidation of benzene and toluene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzene + H(+) + NADH + O2 = cis-1,2-dihydrobenzene-1,2-diol +
CC NAD(+); Xref=Rhea:RHEA:13813, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16190, ChEBI:CHEBI:16716, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + toluene = (1S,2R)-3-methylcyclohexa-3,5-
CC diene-1,2-diol + NAD(+); Xref=Rhea:RHEA:16737, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15565, ChEBI:CHEBI:17578,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.11;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; benzene degradation; catechol
CC from benzene: step 1/2.
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC -!- PATHWAY: Xenobiotic degradation; xylene degradation.
CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC subunits of the hydroxylase component (BnzA and BnzB), a ferredoxin
CC (BnzC) and a ferredoxin reductase (BnzD).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; J04996; AAA26005.1; -; Genomic_DNA.
DR EMBL; CP000712; ABQ79012.1; -; Genomic_DNA.
DR PIR; A36516; A36516.
DR RefSeq; WP_012052601.1; NC_009512.1.
DR PDB; 3EN1; X-ray; 3.20 A; A=1-450.
DR PDB; 3EQQ; X-ray; 3.20 A; A=1-450.
DR PDBsum; 3EN1; -.
DR PDBsum; 3EQQ; -.
DR AlphaFoldDB; A5W4F2; -.
DR SMR; A5W4F2; -.
DR STRING; 351746.Pput_2881; -.
DR EnsemblBacteria; ABQ79012; ABQ79012; Pput_2881.
DR KEGG; ppf:Pput_2881; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_6; -.
DR OMA; AQVGYNE; -.
DR OrthoDB; 275867at2; -.
DR BRENDA; 1.14.12.11; 5092.
DR UniPathway; UPA00228; -.
DR UniPathway; UPA00272; UER00391.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; A5W4F2; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018619; F:benzene 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0018624; F:toluene dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042184; P:xylene catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase.
FT CHAIN 1..450
FT /note="Benzene 1,2-dioxygenase subunit alpha"
FT /id="PRO_0000314465"
FT DOMAIN 54..163
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 96
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3EQQ"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 271..286
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 289..298
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:3EQQ"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:3EQQ"
FT HELIX 373..386
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:3EN1"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:3EN1"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:3EN1"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:3EN1"
SQ 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
