ID   BEDC1_PSEPU             Reviewed;         450 AA.
AC   Q07944;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Benzene 1,2-dioxygenase subunit alpha;
DE            EC=1.14.12.3;
GN   Name=bedC1;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid pHMT112.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC   STRAIN=ML2;
RX   PubMed=8344526; DOI=10.1016/0378-1119(93)90343-2;
RA   Tan H.-M., Tang H.-Y., Joannou C., Abdel-Wahab N.H., Mason J.R.;
RT   "The Pseudomonas putida ML2 plasmid-encoded genes for benzene dioxygenase
RT   are unusual in codon usage and low in G+C content.";
RL   Gene 130:33-39(1993).
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC       Note=Binds 1 Fe cation. {ECO:0000305};
CC   -!- PATHWAY: Aromatic compound metabolism; benzene degradation; catechol
CC       from benzene: step 1/2.
CC   -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC       subunits of the hydroxylase component (BedC1 and BedC2), a ferredoxin
CC       (BedB) and a ferredoxin reductase (BedA).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000305}.
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DR   EMBL; AF148496; AAA17758.1; -; Genomic_DNA.
DR   PIR; JN0812; JN0812.
DR   AlphaFoldDB; Q07944; -.
DR   SMR; Q07944; -.
DR   BioCyc; MetaCyc:MON-12880; -.
DR   UniPathway; UPA00272; UER00391.
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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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; Aromatic hydrocarbons catabolism; Dioxygenase;
KW   Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Oxidoreductase; Plasmid.
FT   CHAIN           1..450
FT                   /note="Benzene 1,2-dioxygenase subunit alpha"
FT                   /id="PRO_0000085044"
FT   DOMAIN          56..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;  51109 MW;  1ECD5EA6C4CF72C8 CRC64;
     MNQTETTPIR VRKNWKTSEI ETLFDEQAGR IDPRIYTDED LYQLELERVF ARSWLLLGHE
     THIRKPGDYF TTYMGEDPVV VVRQKDASIA VFLNQCRHRG MRICRSDAGN AKAFTCSYHG
     WAYDTAGNLI NVPYEAESFA CLDKKEWSPL KARVETYKGL IFANWDENAI DLDTYLGEAK
     FYMDHMLDRT EAGTEVIPGI QKWVIPCNWK FAAEQFCSDM YHAGTTAHLS GIIAGLPEDL
     ELADLAPPKF GKQYRASWGG HGSGFYIGDP NMMLAMMGPK VTSYLTEGPA AEKAAERLGS
     IERGTKIMLE HMTVFPTCSF LPGVNTIRTW HPRGPNEVEV WAFTVVDADA PDDIKEEFRR
     QTLRTFSAGG VFEQDDGENW VEIQHILRGH KARSRPFNAE MSMGQTVDND PIYPGRISNN
     VYSEEAARGL YAHWLKMMTS PDWEALKATR