CARAD_PSERE
ID CARAD_PSERE Reviewed; 329 AA.
AC Q8GI14;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ferredoxin--NAD(P)(+) reductase CarAd;
DE EC=1.18.1.2;
DE EC=1.18.1.3;
DE AltName: Full=Carbazole 1,9a-dioxygenase, ferredoxin reductase component;
DE Short=CARDO;
GN Name=carAd;
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 REDUCTASE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, 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 It can use both NAD and NADP as electron donors, but NAD is supposed to
CC be the physiological electron donor. {ECO:0000269|PubMed:12450807,
CC ECO:0000269|PubMed:9244274}.
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 Evidence={ECO:0000269|PubMed:12450807};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2;
CC Evidence={ECO:0000269|PubMed:12450807};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000305|PubMed:12450807};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000305|PubMed:12450807};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:12450807};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:12450807};
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}.
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DR EMBL; AB047548; BAB32772.1; -; Genomic_DNA.
DR EMBL; AB088420; BAC41551.1; -; Genomic_DNA.
DR RefSeq; NP_758573.1; NC_004444.1.
DR RefSeq; WP_011077884.1; NC_004444.1.
DR AlphaFoldDB; Q8GI14; -.
DR SMR; Q8GI14; -.
DR BRENDA; 1.14.12.22; 7692.
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:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IDA:UniProtKB.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0046232; P:carbazole catabolic process; IDA:UniProtKB.
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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
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 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; Dioxygenase; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; NAD; NADP; Oxidoreductase; Plasmid.
FT CHAIN 1..329
FT /note="Ferredoxin--NAD(P)(+) reductase CarAd"
FT /id="PRO_0000419026"
FT DOMAIN 2..92
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 100..200
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 35
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 329 AA; 36104 MW; 4F659F1B5B55E398 CRC64;
MYQLKIEGQA PGTCGSGKSL LVSALANGIG FPYECASGGC GVCKFELLEG NVQSMWPDAP
GLSSRDREKG NRHLACQCVA LSDLRIKVAV QDKYVPTIPI SRMEAEVVEV RALTHDLLSV
RLRTDGPANF LPGQFCLVEA EQLPGVVRAY SMANLKNPEG IWEFYIKRVP TGRFSPWLFE
NRKEGARLFL TGPMGTSFFR PGTGRKSLCI GGGAGLSYAA AIARASMRET DKPVKLFYGS
RTPRDAVRWI DIDIDEDKLE VVQAVTEDTD SLWQGPTGFI HQVVDAALLE TLPEYEIYLA
GPPPMVDATV RMLLGKGVPR DQIHFDAFF
