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CARAA_PSERE
ID   CARAA_PSERE             Reviewed;         384 AA.
AC   Q8G8B6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Carbazole 1,9a-dioxygenase, terminal oxygenase component CarAa;
DE            Short=CARDO;
DE            EC=1.14.12.22;
GN   Name=carAa;
OS   Pseudomonas resinovorans.
OG   Plasmid pCAR1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=53412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NOMENCLATURE.
RC   STRAIN=CA10;
RX   PubMed=9244273; DOI=10.1128/jb.179.15.4841-4849.1997;
RA   Sato S.I., Ouchiyama N., Kimura T., Nojiri H., Yamane H., Omori T.;
RT   "Cloning of genes involved in carbazole degradation of Pseudomonas sp.
RT   strain CA10: nucleotide sequences of genes and characterization of meta-
RT   cleavage enzymes and hydrolase.";
RL   J. Bacteriol. 179:4841-4849(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN THE CARBAZOLE DEGRADATION,
RP   AND SUBSTRATE SPECIFICITY.
RC   STRAIN=CA10;
RX   PubMed=9244274; DOI=10.1128/jb.179.15.4850-4858.1997;
RA   Sato S.I., Nam J.W., Kasuga K., Nojiri H., Yamane H., Omori T.;
RT   "Identification and characterization of genes encoding carbazole 1,9a-
RT   dioxygenase in Pseudomonas sp. strain CA10.";
RL   J. Bacteriol. 179:4850-4858(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CA10;
RX   PubMed=11371531; DOI=10.1128/jb.183.12.3663-3679.2001;
RA   Nojiri H., Sekiguchi H., Maeda K., Urata M., Nakai S., Yoshida T., Habe H.,
RA   Omori T.;
RT   "Genetic characterization and evolutionary implications of a car gene
RT   cluster in the carbazole degrader Pseudomonas sp. strain CA10.";
RL   J. Bacteriol. 183:3663-3679(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=12547188; DOI=10.1016/s0022-2836(02)01400-6;
RA   Maeda K., Nojiri H., Shintani M., Yoshida T., Habe H., Omori T.;
RT   "Complete nucleotide sequence of carbazole/dioxin-degrading plasmid pCAR1
RT   in Pseudomonas resinovorans strain CA10 indicates its mosaicity and the
RT   presence of large catabolic transposon Tn4676.";
RL   J. Mol. Biol. 326:21-33(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CA10; PLASMID=pCAR1;
RX   PubMed=15466034; DOI=10.1128/jb.186.20.6815-6823.2004;
RA   Urata M., Miyakoshi M., Kai S., Maeda K., Habe H., Omori T., Yamane H.,
RA   Nojiri H.;
RT   "Transcriptional regulation of the ant operon, encoding two-component
RT   anthranilate 1,2-dioxygenase, on the carbazole-degradative plasmid pCAR1 of
RT   Pseudomonas resinovorans strain CA10.";
RL   J. Bacteriol. 186:6815-6823(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=16672459; DOI=10.1128/aem.72.5.3206-3216.2006;
RA   Shintani M., Yano H., Habe H., Omori T., Yamane H., Tsuda M., Nojiri H.;
RT   "Characterization of the replication, maintenance, and transfer features of
RT   the IncP-7 plasmid pCAR1, which carries genes involved in carbazole and
RT   dioxin degradation.";
RL   Appl. Environ. Microbiol. 72:3206-3216(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=17675379; DOI=10.1128/jb.00684-07;
RA   Miyakoshi M., Shintani M., Terabayashi T., Kai S., Yamane H., Nojiri H.;
RT   "Transcriptome analysis of Pseudomonas putida KT2440 harboring the
RT   completely sequenced IncP-7 plasmid pCAR1.";
RL   J. Bacteriol. 189:6849-6860(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=19376894; DOI=10.1128/aem.02373-08;
RA   Takahashi Y., Shintani M., Li L., Yamane H., Nojiri H.;
RT   "Carbazole-degradative IncP-7 plasmid pCAR1.2 is structurally unstable in
RT   Pseudomonas fluorescens Pf0-1, which accumulates catechol, the intermediate
RT   of the carbazole degradation pathway.";
RL   Appl. Environ. Microbiol. 75:3920-3929(2009).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=19270415; DOI=10.1271/bbb.80665;
RA   Takahashi Y., Shintani M., Yamane H., Nojiri H.;
RT   "The complete nucleotide sequence of pCAR2: pCAR2 and pCAR1 were
RT   structurally identical IncP-7 carbazole degradative plasmids.";
RL   Biosci. Biotechnol. Biochem. 73:744-746(2009).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=19134166; DOI=10.1186/1471-2164-10-12;
RA   Miyakoshi M., Nishida H., Shintani M., Yamane H., Nojiri H.;
RT   "High-resolution mapping of plasmid transcriptomes in different host
RT   bacteria.";
RL   BMC Genomics 10:12-12(2009).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=19930443; DOI=10.1111/j.1462-2920.2009.02110.x;
RA   Shintani M., Takahashi Y., Tokumaru H., Kadota K., Hara H., Miyakoshi M.,
RA   Naito K., Yamane H., Nishida H., Nojiri H.;
RT   "Response of the Pseudomonas host chromosomal transcriptome to carriage of
RT   the IncP-7 plasmid pCAR1.";
RL   Environ. Microbiol. 12:1413-1426(2010).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pCAR1;
RX   PubMed=20639326; DOI=10.1128/jb.00591-10;
RA   Yun C.S., Suzuki C., Naito K., Takeda T., Takahashi Y., Sai F.,
RA   Terabayashi T., Miyakoshi M., Shintani M., Nishida H., Yamane H.,
RA   Nojiri H.;
RT   "Pmr, a histone-like protein H1 (H-NS) family protein encoded by the IncP-7
RT   plasmid pCAR1, is a key global regulator that alters host function.";
RL   J. Bacteriol. 192:4720-4731(2010).
RN   [13]
RP   PROTEIN SEQUENCE OF 2-16, FUNCTION AS A TERMINAL OXYGENASE, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=12450807; DOI=10.1128/aem.68.12.5882-5890.2002;
RA   Nam J.W., Nojiri H., Noguchi H., Uchimura H., Yoshida T., Habe H.,
RA   Yamane H., Omori T.;
RT   "Purification and characterization of carbazole 1,9a-dioxygenase, a three-
RT   component dioxygenase system of Pseudomonas resinovorans strain CA10.";
RL   Appl. Environ. Microbiol. 68:5882-5890(2002).
CC   -!- FUNCTION: Part of the multicomponent carbazole 1,9a-dioxygenase
CC       (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol.
CC       Catalyzes the dioxygenation at the angular (C-9a) and adjacent (C-1)
CC       positions of carbazole to yield a highly unstable cis-hydrodiol
CC       intermediate which is spontaneously converted to 2-aminobiphenyl-2,3-
CC       diol. It is also able to attack the angular position adjacent of hetero
CC       atom of heterocyclic aromatic compounds such as polychlorinated
CC       dibenzo-p-dioxin (DD) and dibenzofuran (DBF). It was also shown that
CC       CARDO has the ability to metabolize biphenyl and polycyclic aromatic
CC       hydrocarbons, such as naphthalene and phenanthrene.
CC       {ECO:0000269|PubMed:12450807, ECO:0000269|PubMed:9244274}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9H-carbazole + H(+) + NADH + O2 = 2'-aminobiphenyl-2,3-diol +
CC         NAD(+); Xref=Rhea:RHEA:27838, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:27543, ChEBI:CHEBI:29010, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.14.12.22;
CC         Evidence={ECO:0000269|PubMed:12450807};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9H-carbazole + H(+) + NADPH + O2 = 2'-aminobiphenyl-2,3-diol +
CC         NADP(+); Xref=Rhea:RHEA:27842, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:27543, ChEBI:CHEBI:29010, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.14.12.22;
CC         Evidence={ECO:0000269|PubMed:12450807};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000305};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 7 and 7.5. {ECO:0000269|PubMed:12450807};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:12450807};
CC   -!- SUBUNIT: Homotrimer. Carbazole 1,9a-dioxygenase complex consists of a
CC       terminal oxygenase component CarAa, a ferredoxin reductase component
CC       CarAd and a ferredoxin component CarAc. {ECO:0000269|PubMed:12450807}.
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DR   EMBL; AB047548; BAB32765.1; -; Genomic_DNA.
DR   EMBL; AB047548; BAB32766.1; -; Genomic_DNA.
DR   EMBL; AB088420; BAC41544.1; -; Genomic_DNA.
DR   EMBL; AB088420; BAC41545.1; -; Genomic_DNA.
DR   RefSeq; NP_758566.1; NC_004444.1.
DR   RefSeq; WP_011077878.1; NC_004444.1.
DR   AlphaFoldDB; Q8G8B6; -.
DR   SMR; Q8G8B6; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR   GO; GO:0018564; F:carbazole 1,9a-dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046232; P:carbazole catabolic process; IDA:UniProtKB.
DR   InterPro; IPR021028; Homotrim_ring_OHase_catalytic.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF11723; Aromatic_hydrox; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Dioxygenase; Direct protein sequencing; Iron; Iron-sulfur;
KW   Metal-binding; NAD; NADP; Oxidoreductase; Plasmid.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12450807"
FT   CHAIN           2..384
FT                   /note="Carbazole 1,9a-dioxygenase, terminal oxygenase
FT                   component CarAa"
FT                   /id="PRO_0000419024"
FT   DOMAIN          29..135
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         69
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         71
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         90
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         93
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   384 AA;  43785 MW;  E941848321A6A728 CRC64;
     MANVDEAILK RVKGWAPYVD AKLGFRNHWY PVMFSKEIDE GEPKTLKLLG ENLLVNRIDG
     KLYCLKDRCL HRGVQLSVKV ECKTKSTITC WYHAWTYRWE DGVLCDILTN PTSAQIGRQK
     LKTYPVQEAK GCVFIYLGDG DPPPLARDTP PNFLDDDMEI LGKNQIIKSN WRLAVENGFD
     PSHIYIHKDS ILVKDNDLAL PLGFAPGGDR KQQTRVVDDD VVGRKGVYDL IGEHGVPVFE
     GTIGGEVVRE GAYGEKIVAN DISIWLPGVL KVNPFPNPDM MQFEWYVPID ENTHYYFQTL
     GKPCANDEER KNYEQEFESK WKPMALEGFN NDDIWAREAM VDFYADDKGW VNEILFEVDE
     AIVAWRKLAS EHNQGIQTQA HVSG
 
 
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