(data stored in ACNUC15324 zone)

HOGENOM: ACIAD_1_PE1315

ID   ACIAD_1_PE1315                       STANDARD;      PRT;   338 AA.
AC   ACIAD_1_PE1315; P07771; Q6FCA9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Benzoate 1,2-dioxygenase electron transfer
DE   component;Includes: RecName: Full=Ferredoxin;Includes: RecName:
DE   Full=Ferredoxin--NAD(+) reductase; EC=1.18.1 3; (ACIAD_1.PE1315).
GN   Name=benC; OrderedLocusNames=ACIAD1438;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE1315.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:BENC_ACIAD
CC   -!- FUNCTION: Electron transfer component of benzoate 1,2-dioxygenase
CC       system.
CC   -!- CATALYTIC ACTIVITY: Reduced ferredoxin + NAD(+) = oxidized
CC       ferredoxin + NADH.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- SUBUNIT: This dioxygenase system consists of three proteins: the
CC       two subunits of the hydroxylase component (BenA and BenB), and an
CC       electron transfer component (BenC).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase ferredoxin reductase family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC   -!- GENE_FAMILY: HOG000263663 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P07771; Q6FCA9; -.
DR   EMBL; AF009224; AAC46438.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68302.1; -; Genomic_DNA.
DR   PIR; S23479; S23479.
DR   RefSeq; YP_046124.2; NC_005966.1.
DR   PDB; 1KRH; X-ray; 1.50 A; A/B=11-338.
DR   PDBsum; 1KRH; -.
DR   ProteinModelPortal; P07771; -.
DR   SMR; P07771; 12-348.
DR   STRING; P07771; -.
DR   GeneID; 2880892; -.
DR   GenomeReviews; CR543861_GR; ACIAD1438.
DR   KEGG; aci:ACIAD1438; -.
DR   NMPDR; fig|62977.3.peg.796; -.
DR   eggNOG; COG0543; -.
DR   OMA; NYYRLTI; -.
DR   PhylomeDB; P07771; -.
DR   ProtClustDB; CLSK2329305; -.
DR   BioCyc; ASP62977:ACIAD1438-MON; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_ferredoxin-type.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR008333; OxRdtase_FAD-bd_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR001221; Phe_hydroxylase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; Ferredoxin; 1.
DR   SUPFAM; SSF63380; Riboflavin_synthase_like_b-brl; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   HOGENOMDNA; ACIAD_1.PE1315; -.
KW   2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism;
KW   Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; NAD; Oxidoreductase.
SQ   SEQUENCE   338 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     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
//

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