ID Q7VWV0_BORPE Unreviewed; 418 AA.
AC Q7VWV0;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Dioxygenase hydroxylase component {ECO:0000313|EMBL:CAE42369.1};
GN OrderedLocusNames=BP2091 {ECO:0000313|EMBL:CAE42369.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE42369.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; BX640417; CAE42369.1; -; Genomic_DNA.
DR RefSeq; NP_880751.1; NC_002929.2.
DR RefSeq; WP_010930733.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VWV0; -.
DR STRING; 257313.BP2091; -.
DR PaxDb; 257313-BP2091; -.
DR GeneID; 69601860; -.
DR KEGG; bpe:BP2091; -.
DR PATRIC; fig|257313.5.peg.2250; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_4; -.
DR Proteomes; UP000002676; 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:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd08879; RHO_alpha_C_AntDO-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:CAE42369.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002676}.
FT DOMAIN 42..116
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 418 AA; 47626 MW; F28173B03B0AD347 CRC64;
MSFIRNEIDY RALIEPTRIN SRLYVDPEIF QEELDKIWHR TWVYVGHVSE VPNKNDYVTK
SIGTTPVLLL RDRDGEIRLL LNKCPHRGNQ LCAYKEGNRS TFTCPYHSWT FSNTGDLMGY
ALADGYEGAS KAGVGLGKVA RIGIYRGFVF GSFAETGPSL DEHLGGAKAA IDQLCDNSPN
GELDLRAGFL QHRAKANWKF MLENETDGYH PGFVHGSIFQ VTNSPIANLY GKDSTALTRD
YGNGHTEFDL RPEWRRIDKP LYWFGSSVER MADYAVAMDQ AYGAERARQI MIDGSPHTMI
FPNLFIAEIQ IFVLQPVSVE ETIQHVTAVQ FKDAPDINRR LRQQTMGSVG PAGLLLADDT
EMYERNHRGA KIRDPEWLML TRGLHRERKD ENGYTVGHST DEVPQRGIWR HYFKLMQE
//
