ID A0A196NE07_9SPHN Unreviewed; 464 AA.
AC A0A196NE07;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Benzoate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:OAN65725.1};
GN ORFNames=A7X12_15540 {ECO:0000313|EMBL:OAN65725.1};
OS Sphingomonas sp. TDK1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=453247 {ECO:0000313|EMBL:OAN65725.1, ECO:0000313|Proteomes:UP000078445};
RN [1] {ECO:0000313|EMBL:OAN65725.1, ECO:0000313|Proteomes:UP000078445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDK1 {ECO:0000313|EMBL:OAN65725.1,
RC ECO:0000313|Proteomes:UP000078445};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAN65725.1}.
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DR EMBL; LXVY01000006; OAN65725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A196NE07; -.
DR STRING; 453247.A7X12_15540; -.
DR OrthoDB; 7456916at2; -.
DR Proteomes; UP000078445; Unassembled WGS sequence.
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:OAN65725.1};
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}.
FT DOMAIN 50..147
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 464 AA; 51396 MW; 421D5E9A6FDDCB4D CRC64;
MIVTSTLAER IAGAVIDDPE AGLFRCRRDV FTDPALFDLE MKHIFEGNWV YLAHESQIPE
PNDYFTTWIG RTPIIVTRDK GGELHAFVNA CAHRGATLCR RKHGNKGSFT CPFHGWTFSN
TGRLLKVKDG KSGGYPDAFD TGGLHDLTRV ARFESYRGFL FGSLRTEVQP LAEYLGATRT
IIDQIVDQAP DGIEVLRGNS TYVYDGNWKL QIENGADGYH VSTVHWNYAA TMAHRDYDAA
GTRTVDANGW SKSVGGVYGF ENGHILLWTR LLNPEVRPIH AHRESLAARL GEARAAFVVE
QTRNLCLYPN VYLMDQFSTQ IRVVRPISVD RTEVTIYCFA PKGESAAERA LRLRQYEDFF
NVSGMGTPDD LEEFRACQTA YTGAGDLWND LSRGATRWID GPDDNARAMG LEPILSGERS
EDEGLFVRQH EYWAKTLLAA IEAEGGGGGD GAAVSPAASL RAVA
//
