ID A0A238K6P7_9RHOB Unreviewed; 462 AA.
AC A0A238K6P7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=2-halobenzoate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:SMX38591.1};
DE EC=1.14.12.13 {ECO:0000313|EMBL:SMX38591.1};
GN Name=cbdA {ECO:0000313|EMBL:SMX38591.1};
GN ORFNames=MAA8898_01620 {ECO:0000313|EMBL:SMX38591.1};
OS Maliponia aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Maliponia.
OX NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX38591.1, ECO:0000313|Proteomes:UP000207598};
RN [1] {ECO:0000313|EMBL:SMX38591.1, ECO:0000313|Proteomes:UP000207598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX38591.1,
RC ECO:0000313|Proteomes:UP000207598};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; FXYF01000004; SMX38591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238K6P7; -.
DR OrthoDB; 7456916at2; -.
DR Proteomes; UP000207598; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018626; F:2-chlorobenzoate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd08879; RHO_alpha_C_AntDO-like; 1.
DR CDD; cd03542; Rieske_RO_Alpha_HBDO; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017639; Benzo_1-2-diOase_lsu.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR NCBIfam; TIGR03229; benzo_1_2_benA; 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.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:SMX38591.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SMX38591.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000207598}.
FT DOMAIN 53..150
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 462 AA; 52343 MW; A4EF7783F2FD2B05 CRC64;
MFTQSNLDAF EARLDGAIQD DPENGVFRCR RDIFADEELF ELEIKHIFEG NWIYMAHESQ
IPNPGDYFTL TMGRTPVVIT RDKDGELHAL VNACSHRGAQ LCRFKRRNQK TFTCPFHGWT
FSNTGKLLKV KDPKGAGYPE QFNKDGSHDL TKVARFENYR GFLFGSLNAD VKPLEDYLGE
ARKMIDMIVD QADEGLEVLR GSSTYTYDGN WKLQAENGAD GYHVSAVHWN YVATTAHRTD
DGKEDNIKAT DASKWAKQRG GFHAYENGHI LLWTEWADPT NRPNYPRKDE WTEKHGKTKA
DWMVGVLRNL CLYPNVFLMD QFSSQIRVFR PVSVDQTEVT IYCIAPKGES QEARTRRIRQ
YEDFFNASGM ATPDDTEEFR ATQRGYAGAA HAKWNDLTRG ATQWIQGPDE DAKALGIAPI
LSGARTEDEG LFVIQHSNWS QRMADAIAKE RATAPGASVA AE
//