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 04-NOV-2026, entry version 99. 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 / JCM 31910 / BCRC 17059 OS / LMG 24140 / F1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; 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 / JCM 31910 / BCRC 17059 / LMG 24140 / RC 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 + NADH + O2 + H(+) = 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=toluene + NADH + O2 + H(+) = (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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04996; AAA26005.1; -; Genomic_DNA. DR EMBL; CP000712; ABQ79012.1; -; Genomic_DNA. DR PIR; A36516; A36516. DR PDB; 3EN1; X-ray; 3.20 A; A=1-450. DR PDB; 3EQQ; X-ray; 3.20 A; A=1-450. DR SMR; A5W4F2; -. DR KEGG; ppf:Pput_2881; -. DR eggNOG; COG4638; Bacteria. DR HOGENOM; CLU_026244_4_0_6; -. DR OMA; ACAYPHG; -. DR BRENDA; 1.14.12.11; 5092. DR UniPathway; UPA00228; -. DR UniPathway; UPA00272; UER00391. DR UniPathway; UPA00273; -. DR EvolutionaryTrace; A5W4F2; -. DR CDD; cd08881; RHO_alpha_C_NDO-like; 1. DR Gene3D; 3.90.380.10; Naphthalene 1,2-dioxygenase Alpha Subunit, Chain A, domain 1; 1. DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1. DR InterPro; IPR015881; ARHD_Rieske_2Fe_2S. DR InterPro; IPR043266; RHO_NdoB-like_C. DR InterPro; IPR017941; Rieske_2Fe-2S. DR InterPro; IPR036922; Rieske_2Fe-2S_sf. DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom. DR InterPro; IPR001663; Rng_hydr_dOase-A. DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1. DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF00848; Ring_hydroxyl_A; 1. DR PRINTS; PR00090; RNGDIOXGNASE. DR SUPFAM; SSF55961; Bet v1-like; 1. DR SUPFAM; SSF50022; ISP domain; 1. DR PROSITE; PS51296; RIESKE; 1. DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. 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 AlphaFoldDB; A5W4F2; -. 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 //