ID A9IG99_BORPD Unreviewed; 420 AA.
AC A9IG99;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Probable Ring hydroxylating alpha subunit {ECO:0000313|EMBL:CAP41879.1};
DE EC=1.14.12.- {ECO:0000313|EMBL:CAP41879.1};
GN OrderedLocusNames=Bpet1540 {ECO:0000313|EMBL:CAP41879.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP41879.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP41879.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; AM902716; CAP41879.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IG99; -.
DR STRING; 94624.Bpet1540; -.
DR KEGG; bpt:Bpet1540; -.
DR eggNOG; COG4638; Bacteria.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017638; Anthranilate_1-2-diOase_lsu.
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 NCBIfam; NF041684; ant_diox_AndAc; 1.
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};
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 ECO:0000313|EMBL:CAP41879.1}.
FT DOMAIN 50..164
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 420 AA; 47900 MW; F43E770A318C1C52 CRC64;
MSEMVAKPSA HAERTVSFLQ PNGSEVPFRV FSSQEVYDRE QERIFRGATW SFLGLEAEIP
NVYDFKSTFI GDTPVVVTRT PDGLSCWVNR CAHRGAQVCR ELRGNARSHA CVYHQWGYSA
KGDLLGVPFR RGQNGMAGMP ADFKTEEHGL QQVRVASYRG LVFGTFRQDT PSLEDYIGPM
MRPWIDRIFH KPVVYLGCTR QYSKSNWKLY LENVKDGYHA SLLHLFHTTF NIYRVGMKVR
QMADVGGLHS LLTSTKPEVD TNTAAAYEAQ KVRTMNNKLV LEDPTLLGQI QEYEEITTNN
IQAILPQLVI QQIHNTLAAR QLLPKGPNNF ELIFHFFGYE DDTPELRELR LLQANLVGPA
GYISMEDTEA TELVQRATRM DPDSHSYIAM AQDVPEETDS SITEYMIRRF WTSYQALMGY
//
