BOXB_AROEV
ID BOXB_AROEV Reviewed; 473 AA.
AC Q9AIX7;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Benzoyl-CoA oxygenase component B;
DE EC=1.14.13.208 {ECO:0000269|PubMed:15458418};
DE AltName: Full=Benzoyl-CoA 2,3-dioxygenase subunit B;
DE AltName: Full=Benzoyl-CoA dioxygenase oxygenase component;
GN Name=boxB;
OS Aromatoleum evansii (Azoarcus evansii).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=59406;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10, AND INDUCTION.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=11222587; DOI=10.1128/jb.183.6.1899-1908.2001;
RA Mohamed M.E.-S., Zaar A., Ebenau-Jehle C., Fuchs G.;
RT "Reinvestigation of a new type of aerobic benzoate metabolism in the
RT proteobacterium Azoarcus evansii.";
RL J. Bacteriol. 183:1899-1908(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=12399500; DOI=10.1128/jb.184.22.6301-6315.2002;
RA Gescher J., Zaar A., Mohamed M.E.-S., Schaegger H., Fuchs G.;
RT "Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus
RT evansii.";
RL J. Bacteriol. 184:6301-6315(2002).
RN [3]
RP PROTEIN SEQUENCE OF 1-9, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=15458418; DOI=10.1111/j.1365-2958.2004.04263.x;
RA Zaar A., Gescher J., Eisenreich W., Bacher A., Fuchs G.;
RT "New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii.";
RL Mol. Microbiol. 54:223-238(2004).
CC -!- FUNCTION: The BoxA/BoxB complex catalyzes the aerobic
CC reduction/oxygenation of the aromatic ring of benzoyl-CoA to form 2,3-
CC epoxy-2,3-dihydrobenzoyl-CoA. BoxB acts as the benzoyl-CoA oxygenase,
CC after being reduced by the reductase component BoxA. BoxAB does not act
CC on NADH or benzoate. {ECO:0000269|PubMed:15458418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + H(+) + NADPH + O2 = 2,3-epoxy-2,3-
CC dihydrobenzoyl-CoA + H2O + NADP(+); Xref=Rhea:RHEA:48312,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:88118; EC=1.14.13.208;
CC Evidence={ECO:0000269|PubMed:15458418};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:15458418};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for benzoyl-CoA {ECO:0000269|PubMed:15458418};
CC -!- SUBUNIT: Monomer. The subunit composition of the active BoxA/BoxB
CC protein complex is not known. {ECO:0000269|PubMed:15458418}.
CC -!- INDUCTION: By benzoate. {ECO:0000269|PubMed:11222587}.
CC -!- SIMILARITY: Belongs to the benzoyl-CoA oxygenase component B family.
CC {ECO:0000305}.
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DR EMBL; AF220510; AAK00599.1; -; Genomic_DNA.
DR EMBL; AF548005; AAN39376.1; -; Genomic_DNA.
DR PDB; 3PER; X-ray; 2.10 A; A/B=1-473.
DR PDB; 3PF7; X-ray; 1.90 A; A/B=1-473.
DR PDB; 3PM5; X-ray; 2.30 A; A/B/C/D=1-473.
DR PDB; 3Q1G; X-ray; 2.50 A; A/B/C/D=1-473.
DR PDBsum; 3PER; -.
DR PDBsum; 3PF7; -.
DR PDBsum; 3PM5; -.
DR PDBsum; 3Q1G; -.
DR AlphaFoldDB; Q9AIX7; -.
DR SMR; Q9AIX7; -.
DR KEGG; ag:AAN39376; -.
DR BioCyc; MetaCyc:MON-3143; -.
DR BRENDA; 1.14.13.208; 603.
DR SABIO-RK; Q9AIX7; -.
DR EvolutionaryTrace; Q9AIX7; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR017635; Benzoyl_CoA_Oase_BoxB_bsu.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR03225; benzo_boxB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; Iron; Metal-binding; NADP; Oxidoreductase.
FT CHAIN 1..473
FT /note="Benzoyl-CoA oxygenase component B"
FT /id="PRO_0000350727"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 18..38
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3PF7"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 106..127
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 137..164
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 227..265
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 356..382
FT /evidence="ECO:0007829|PDB:3PF7"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3PER"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:3PF7"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 416..422
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:3PF7"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:3PF7"
SQ SEQUENCE 473 AA; 54555 MW; 220452161640EDC8 CRC64;
MINYSERIPN NVNLNENKTL QRALEQWQPS FLNWWDDMGP ENSSNYDVYL RTAVSVDPKG
WADFGYVKMH DYRWGIFLAP QEGEKKITFG EHKGQDVWQE VPGEYRSTLR RIIVTQGDTE
PASVEQQRHL GLTAPSLYDL RNLFQVNVEE GRHLWAMVYL LHAHFGRDGR EEGEALLERR
SGDEDNPRIL TAFNEKTPDW LSFFMFTFIT DRDGKFQLAS LAESAFDPLA RTCKFMLTEE
AHHLFVGESG IARVIQRTCE VMKELGTDDP AKLRAAGVID LPTLQKYLNF HYSVTSDLYG
AEISSNAATY YTNGLKGRFE EEKIGDDHKL QNSEYEVMDV AGDKILTRHV PALSALNERL
RDDWITDVQA GVDRWNRIPA KFGFDFRFTL PHKGFHRKIG MFADVHVSPD GRLISEAEWT
HQHKNWLPTE SDRLYVHSLM GRCLEPGKFA NWIAAPARGI NNQPVNFEYV RFN
