ID Q0SCI2_RHOJR Unreviewed; 323 AA.
AC Q0SCI2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Phthalate dioxygenase reductase {ECO:0000313|EMBL:ABG94754.1};
GN OrderedLocusNames=RHA1_ro02949 {ECO:0000313|EMBL:ABG94754.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94754.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000431; ABG94754.1; -; Genomic_DNA.
DR RefSeq; WP_011595627.1; NC_008268.1.
DR AlphaFoldDB; Q0SCI2; -.
DR KEGG; rha:RHA1_ro02949; -.
DR PATRIC; fig|101510.16.peg.2980; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_11; -.
DR OrthoDB; 502624at2; -.
DR Proteomes; UP000008710; Chromosome.
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; 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:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 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:ABG94754.1};
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:ABG94754.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 11..113
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 238..323
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 323 AA; 34308 MW; C0E554063E2107F1 CRC64;
MPQNPVSSGA PANAALQVVA KEVVAESVVA LTLRHPDGRR LPDWAPGAHI DLLLPNGLTR
QYSLCGDRWD AYSYRVGVLR EPAGRGGSAY VHDVLAEGDL VGVGGPRNNF PLVPAPRYLF
IAGGIGITPL LPMVRQAELM GIDWQLLYGG RTRTSMAFRD ELAAYGDRVS VVPRDEQGHL
DLSAHLAAEA ADAKVYVCGP GPLLAAVENC CTDWPVGTLR TERFVPKDNG VPLRDEPFEV
ELARSGLAVT VTPGASVLDA VQAAGVDVLS SCREGTCGTC ETTVLAGAPD HRDSVLDDEE
RSAGDCMLIC VSRSCSDRLV LDL
//
