BNZA_PSEPU
ID BNZA_PSEPU Reviewed; 450 AA.
AC P0C618; P08084; P13450;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
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;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BE-81;
RX PubMed=3667527; DOI=10.1128/jb.169.11.5174-5179.1987;
RA Irie S., Doi S., Yorifuji T., Takagi M., Yano K.;
RT "Nucleotide sequencing and characterization of the genes encoding benzene
RT oxidation enzymes of Pseudomonas putida.";
RL J. Bacteriol. 169:5174-5179(1987).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25735.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M17904; AAA25735.1; ALT_FRAME; Genomic_DNA.
DR PIR; A29830; A29830.
DR RefSeq; WP_012052601.1; NZ_NHBC01000013.1.
DR AlphaFoldDB; P0C618; -.
DR SMR; P0C618; -.
DR UniPathway; UPA00228; -.
DR UniPathway; UPA00272; UER00391.
DR UniPathway; UPA00273; -.
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 3: Inferred from homology;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..450
FT /note="Benzene 1,2-dioxygenase subunit alpha"
FT /id="PRO_0000085045"
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"
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
