BENC_ACIAD
ID BENC_ACIAD Reviewed; 348 AA.
AC P07771; Q6FCA9;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Benzoate 1,2-dioxygenase electron transfer component;
DE Includes:
DE RecName: Full=Ferredoxin;
DE Includes:
DE RecName: Full=Ferredoxin--NAD(+) reductase;
DE EC=1.18.1.3;
GN Name=benC; OrderedLocusNames=ACIAD1438;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1885518; DOI=10.1128/jb.173.17.5385-5395.1991;
RA Neidle E.L., Hartnett C., Ornston N.L., Bairoch A., Rekik M., Harayama S.;
RT "Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for
RT benzoate 1,2-dioxygenase reveal evolutionary relationships among
RT multicomponent oxygenases.";
RL J. Bacteriol. 173:5385-5395(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Electron transfer component of benzoate 1,2-dioxygenase
CC system.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC -!- SUBUNIT: This dioxygenase system consists of three proteins: the two
CC subunits of the hydroxylase component (BenA and BenB), and an electron
CC transfer component (BenC).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF009224; AAC46438.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68302.1; -; Genomic_DNA.
DR PIR; S23479; S23479.
DR PDB; 1KRH; X-ray; 1.50 A; A/B=11-348.
DR PDBsum; 1KRH; -.
DR AlphaFoldDB; P07771; -.
DR SMR; P07771; -.
DR STRING; 62977.ACIAD1438; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR EnsemblBacteria; CAG68302; CAG68302; ACIAD1438.
DR KEGG; aci:ACIAD1438; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG0633; Bacteria.
DR HOGENOM; CLU_003827_7_0_6; -.
DR OMA; GTCKCHC; -.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; P07771; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..348
FT /note="Benzoate 1,2-dioxygenase electron transfer
FT component"
FT /id="PRO_0000167655"
FT DOMAIN 14..109
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 116..217
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 111..348
FT /note="Ferredoxin-reductase"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 59
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT CONFLICT 29
FT /note="R -> C (in Ref. 1; AAC46438)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="A -> E (in Ref. 1; AAC46438)"
FT /evidence="ECO:0000305"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1KRH"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1KRH"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 117..140
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:1KRH"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:1KRH"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:1KRH"
SQ SEQUENCE 348 AA; 38783 MW; AAD68A290C7D51F6 CRC64;
MSLYLNRIPA MSNHQVALQF EDGVTRFIRI AQGETLSDAA YRQQINIPMD CREGACGTCR
AFCESGNYDM PEDNYIEDAL TPEEAQQGYV LACQCRPTSD AVFQIQASSE VCKTKIHHFE
GTLARVENLS DSTITFDIQL DDGQPDIHFL AGQYVNVTLP GTTETRSYSF SSQPGNRLTG
FVVRNVPQGK MSEYLSVQAK AGDKMSFTGP FGSFYLRDVK RPVLMLAGGT GIAPFLSMLQ
VLEQKGSEHP VRLVFGVTQD CDLVALEQLD ALQQKLPWFE YRTVVAHAES QHERKGYVTG
HIEYDWLNGG EVDVYLCGPV PMVEAVRSWL DTQGIQPANF LFEKFSAN
