ID B7XGD9_PSEPU Unreviewed; 314 AA.
AC B7XGD9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Reductase component of dioxygenase system {ECO:0000313|EMBL:BAH09947.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pCAR1.2 {ECO:0000313|EMBL:BAH09947.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303 {ECO:0000313|EMBL:BAH09947.1};
RN [1] {ECO:0000313|EMBL:BAH09947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA10 {ECO:0000313|EMBL:BAH09947.1};
RC PLASMID=pCAR1.2 {ECO:0000313|EMBL:BAH09947.1};
RA Shintani M., Yoshida T., Habe H., Omori T., Nojiri H.;
RT "Large plasmid pCAR2 and class II transposon Tn4676 are functional mobile
RT genetic elements to distribute the carbazole/dioxin-degradative car gene
RT cluster in different bacteria.";
RL Appl. Microbiol. Biotechnol. 67:370-382(2005).
RN [2] {ECO:0000313|EMBL:BAH09947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA10 {ECO:0000313|EMBL:BAH09947.1};
RC PLASMID=pCAR1.2 {ECO:0000313|EMBL:BAH09947.1};
RA Shintani M., Habe H., Tsuda M., Omori T., Yamane H., Nojiri H.;
RT "Recipient range of IncP-7 conjugative plasmid pCAR2 from Pseudomonas
RT putida HS01 is broader than from other Pseudomonas strains.";
RL Biotechnol. Lett. 27:1847-1853(2005).
RN [3] {ECO:0000313|EMBL:BAH09947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA10 {ECO:0000313|EMBL:BAH09947.1};
RC PLASMID=pCAR1.2 {ECO:0000313|EMBL:BAH09947.1};
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 [4] {ECO:0000313|EMBL:BAH09947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA10 {ECO:0000313|EMBL:BAH09947.1};
RC PLASMID=pCAR1.2 {ECO:0000313|EMBL:BAH09947.1};
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 [5] {ECO:0000313|EMBL:BAH09947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA10 {ECO:0000313|EMBL:BAH09947.1};
RC PLASMID=pCAR1.2 {ECO:0000313|EMBL:BAH09947.1};
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 [6] {ECO:0000313|EMBL:BAH09947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA10 {ECO:0000313|EMBL:BAH09947.1};
RC PLASMID=pCAR1.2 {ECO:0000313|EMBL:BAH09947.1};
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 [7] {ECO:0000313|EMBL:BAH09947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA10 {ECO:0000313|EMBL:BAH09947.1};
RC PLASMID=pCAR1.2 {ECO:0000313|EMBL:BAH09947.1};
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).
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DR EMBL; AB474758; BAH09947.1; -; Genomic_DNA.
DR RefSeq; WP_011077870.1; NC_011838.1.
DR RefSeq; YP_002473960.1; NC_011838.1.
DR AlphaFoldDB; B7XGD9; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF2; PHENOXYBENZOATE DIOXYGENASE BETA SUBUNIT; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:BAH09947.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000313|EMBL:BAH09947.1};
KW Plasmid {ECO:0000313|EMBL:BAH09947.1}.
FT DOMAIN 1..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 230..314
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 314 AA; 33885 MW; 6C7BAC698D978FB5 CRC64;
MPSLSLRIER IDPLTPRIRR LILVADAQQP LPGFTPGAHI EIQIAGSKPQ WRAYSLVNLP
GHAHYEIAVQ LEEQSSGGSR WIHQLQVGQP LQVRAPKNHF PLVTQASDYL LIAGGIGITP
MLGMARALAA GQQPFTLHYA GREAQGMAYL EEVRALGSAH CWISGGDPAR RLPLASLLAT
PHNGRQLYVC GPKALIASVL HSARELGWDD SHVHSELFTG SLDAAGDASF EVELRSSGIT
LQVPAGKSVL EAMLDADLDP LFDCRRGDCG VCVAQVLEGS AEHRDICLSA RERSDGRFCT
CVSRASSARL VLDL
//
