位置:首页 > 蛋白库 > CARAC_PSERE
CARAC_PSERE
ID   CARAC_PSERE             Reviewed;         107 AA.
AC   Q8GI16;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ferredoxin CarAc;
DE   AltName: Full=Carbazole 1,9a-dioxygenase, ferredoxin component;
DE            Short=CARDO;
GN   Name=carAc;
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], AND FUNCTION IN THE CARBAZOLE
RP   DEGRADATION.
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 1-15, FUNCTION AS A FERREDOXIN, BIOPHYSICOCHEMICAL
RP   PROPERTIES, COFACTOR, AND SUBUNIT.
RC   STRAIN=CA10;
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).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP   (2FE-2S).
RC   STRAIN=CA10;
RX   PubMed=15645447; DOI=10.1002/prot.20374;
RA   Nam J.W., Noguchi H., Fujimoto Z., Mizuno H., Ashikawa Y., Abo M.,
RA   Fushinobu S., Kobashi N., Wakagi T., Iwata K., Yoshida T., Habe H.,
RA   Yamane H., Omori T., Nojiri H.;
RT   "Crystal structure of the ferredoxin component of carbazole 1,9a-
RT   dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-
RT   heme iron oxygenase system.";
RL   Proteins 58:779-789(2005).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP   (2FE-2S), AND COFACTOR.
RX   PubMed=17161368; DOI=10.1016/j.str.2006.10.004;
RA   Ashikawa Y., Fujimoto Z., Noguchi H., Habe H., Omori T., Yamane H.,
RA   Nojiri H.;
RT   "Electron transfer complex formation between oxygenase and ferredoxin
RT   components in Rieske nonheme iron oxygenase system.";
RL   Structure 14:1779-1789(2006).
CC   -!- FUNCTION: Part of the multicomponent carbazole 1,9a-dioxygenase
CC       (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol.
CC       Acts as a mediator in the electron transfer from CarAd to CarAa.
CC       {ECO:0000269|PubMed:12450807, ECO:0000269|PubMed:9244274}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628,
CC         ECO:0000269|PubMed:12450807, ECO:0000269|PubMed:17161368};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628, ECO:0000269|PubMed:12450807,
CC       ECO:0000269|PubMed:17161368};
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: Monomer. 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,
CC       ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB047548; BAB32770.1; -; Genomic_DNA.
DR   EMBL; AB088420; BAC41549.1; -; Genomic_DNA.
DR   RefSeq; NP_758571.1; NC_004444.1.
DR   RefSeq; WP_011077882.1; NC_004444.1.
DR   PDB; 1VCK; X-ray; 1.90 A; A=1-107.
DR   PDB; 2DE5; X-ray; 1.90 A; D/E/F=1-107.
DR   PDB; 2DE6; X-ray; 1.80 A; D/E/F=1-107.
DR   PDB; 2DE7; X-ray; 2.00 A; D/E/F=1-107.
DR   PDB; 3VMG; X-ray; 1.95 A; D/E/F=1-107.
DR   PDB; 3VMH; X-ray; 1.85 A; D/E/F=1-107.
DR   PDB; 3VMI; X-ray; 2.00 A; D/E/F=1-107.
DR   PDB; 4NB8; X-ray; 2.01 A; D/E/F=1-107.
DR   PDB; 4NB9; X-ray; 2.05 A; D/E/F=1-107.
DR   PDB; 4NBA; X-ray; 2.10 A; D/E/F=1-107.
DR   PDB; 4NBB; X-ray; 2.05 A; D/E/F=1-107.
DR   PDB; 4NBC; X-ray; 1.94 A; D/E/F=1-107.
DR   PDB; 4NBD; X-ray; 1.95 A; D/E=1-107.
DR   PDB; 4NBE; X-ray; 2.10 A; D/E=1-107.
DR   PDB; 4NBF; X-ray; 2.00 A; D/E/F=1-107.
DR   PDB; 4NBG; X-ray; 1.85 A; D/E/F=1-107.
DR   PDB; 4NBH; X-ray; 2.15 A; D/E/F=1-107.
DR   PDB; 6LLF; X-ray; 1.93 A; D/E/F=1-107.
DR   PDB; 6LLH; X-ray; 1.99 A; D/E/F=1-107.
DR   PDB; 7BUH; X-ray; 1.79 A; A=1-107.
DR   PDB; 7BUI; X-ray; 2.15 A; D/E=1-107.
DR   PDBsum; 1VCK; -.
DR   PDBsum; 2DE5; -.
DR   PDBsum; 2DE6; -.
DR   PDBsum; 2DE7; -.
DR   PDBsum; 3VMG; -.
DR   PDBsum; 3VMH; -.
DR   PDBsum; 3VMI; -.
DR   PDBsum; 4NB8; -.
DR   PDBsum; 4NB9; -.
DR   PDBsum; 4NBA; -.
DR   PDBsum; 4NBB; -.
DR   PDBsum; 4NBC; -.
DR   PDBsum; 4NBD; -.
DR   PDBsum; 4NBE; -.
DR   PDBsum; 4NBF; -.
DR   PDBsum; 4NBG; -.
DR   PDBsum; 4NBH; -.
DR   PDBsum; 6LLF; -.
DR   PDBsum; 6LLH; -.
DR   PDBsum; 7BUH; -.
DR   PDBsum; 7BUI; -.
DR   AlphaFoldDB; Q8GI16; -.
DR   SMR; Q8GI16; -.
DR   DIP; DIP-29166N; -.
DR   IntAct; Q8GI16; 1.
DR   DrugBank; DB07301; Carbazole.
DR   BRENDA; 1.14.12.22; 7692.
DR   EvolutionaryTrace; Q8GI16; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008901; F:ferredoxin hydrogenase 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   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Dioxygenase; Direct protein sequencing; Iron;
KW   Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..107
FT                   /note="Ferredoxin CarAc"
FT                   /id="PRO_0000419028"
FT   DOMAIN          6..102
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         46
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT                   ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368"
FT   BINDING         48
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT                   ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368"
FT   BINDING         65
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT                   ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368"
FT   BINDING         68
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628,
FT                   ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          19..24
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          27..35
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          38..45
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:7BUH"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:7BUH"
SQ   SEQUENCE   107 AA;  11367 MW;  4B60F233E57C19A4 CRC64;
     MNQIWLKVCA ASDMQPGTIR RVNRVGAAPL AVYRVGDQFY ATEDTCTHGI ASLSEGTLDG
     DVIECPFHGG AFNVCTGMPA SSPCTVPLGV FEVEVKEGEV YVAGEKK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025