BENA_ACIAD
ID BENA_ACIAD Reviewed; 461 AA.
AC P07769;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Benzoate 1,2-dioxygenase subunit alpha;
DE EC=1.14.12.10;
GN Name=benA; OrderedLocusNames=ACIAD1436;
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 SEQUENCE REVISION TO 84; 103-104; 171-172 AND 380-382.
RA Elby D.M., Neidle E.L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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: Degradation of benzoate to 2-hydro-1,2-dihydroxybenzoate
CC (DHB).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoate + H(+) + NADH + O2 = (1R,6S)-1,6-dihydroxycyclohexa-
CC 2,4-diene-1-carboxylate + NAD(+); Xref=Rhea:RHEA:12633,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16150,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60129;
CC EC=1.14.12.10;
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; benzoate degradation via
CC hydroxylation; catechol from benzoate: step 1/2.
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 alpha subunit family. {ECO:0000305}.
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DR EMBL; AF009224; AAC46436.2; -; Genomic_DNA.
DR EMBL; CR543861; CAG68300.1; -; Genomic_DNA.
DR RefSeq; WP_004925496.1; NC_005966.1.
DR AlphaFoldDB; P07769; -.
DR SMR; P07769; -.
DR STRING; 62977.ACIAD1436; -.
DR EnsemblBacteria; CAG68300; CAG68300; ACIAD1436.
DR GeneID; 45233849; -.
DR KEGG; aci:ACIAD1436; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_1_6; -.
DR OMA; TRNLCLY; -.
DR OrthoDB; 275867at2; -.
DR BioCyc; ASP62977:ACIAD_RS06635-MON; -.
DR UniPathway; UPA00156; UER00254.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018623; F:benzoate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017639; Benzo_1-2-diOase_lsu.
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 TIGRFAMs; TIGR03229; benzo_1_2_benA; 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; Reference proteome.
FT CHAIN 1..461
FT /note="Benzoate 1,2-dioxygenase subunit alpha"
FT /id="PRO_0000085043"
FT DOMAIN 54..151
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 95
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 115
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 461 AA; 52229 MW; CFCC3247A3C4C379 CRC64;
MPRIPVINTS HLDRIDELLV DNTETGEFKL HRSVFTDQAL FDLEMKYIFE GNWVYLAHES
QIPNNNDYYT TYIGRQPILI ARNRNGELNA MINACSHRGA QLCRHKRGNK TTYTCPFHGW
TFNNSGKLLK VKDPSDAGYS DCFNQDGSHD LKKVARFESY KGFLFGSLNP DVPSLQEFLG
ETTKIIDMIV GQSDQGLEVL RGVSTYTYEG NWKLTAENGA DGYHVSAVHW NYAATTQHRK
EKQAGDTIRA MSAGSWGKHG GGSYGFEHGH MLLWTQWGNP EDRPNFPKAA EYTEKFGAAM
SKWMIERSRN LCLYPNVYLM DQFGSQIRVL RPISVNKTEV TIYCIAPVGE APEARARRIR
QYEDFFNASG MATPDDLEEF RACQAGYAGI ELEWNDMCRG SKHWIYGPDD AANEIGLKPA
ISGIKTEDEG LYLAQHQYWL KSMKQAIAAE KEFASRQGEN A
