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Database: UniProt
Entry: A0A1H2PK54_9BURK
LinkDB: A0A1H2PK54_9BURK
Original site: A0A1H2PK54_9BURK 
ID   A0A1H2PK54_9BURK        Unreviewed;       428 AA.
AC   A0A1H2PK54;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Anthranilate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:SDV46826.1};
GN   ORFNames=SAMN05216551_10219 {ECO:0000313|EMBL:SDV46826.1};
OS   Chitinasiproducens palmae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Chitinasiproducens.
OX   NCBI_TaxID=1770053 {ECO:0000313|EMBL:SDV46826.1, ECO:0000313|Proteomes:UP000243719};
RN   [1] {ECO:0000313|Proteomes:UP000243719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS23 {ECO:0000313|Proteomes:UP000243719};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2016) 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; FNLO01000002; SDV46826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2PK54; -.
DR   STRING; 1770053.SAMN05216551_10219; -.
DR   OrthoDB; 9790995at2; -.
DR   Proteomes; UP000243719; 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   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:SDV46826.1};
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:UP000243719}.
FT   DOMAIN          40..155
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   428 AA;  48022 MW;  25B01846256876DB CRC64;
     MSVSPITWPA KDFSRVPFSI YHDPAVYLDE LDKIFHGPTW NYLALEAELP NPGDFITTLL
     GETSVIVSRD AEGRVHAFVN RCKHRGATLR REACGNAKSH TCIYHQWAYS LDGRLQSVPF
     AKGMKGEGGL PKDFDKSSIR LDMLTVEVYK GVVFASFSPA AEPLADYLGP AVIAELDRLF
     ARKVKVLGYQ RQRIFGNWKL YNDNVRDPNH GGLLHMFHAT FGLYRLSQVG GAKMDGKHRH
     NITYNQLGSD DTADNAGYDG TTKVFQEGYQ LLDKSMLEYK RDYPDMVSLV ILSVFPSVVF
     QQIANSLCTR QIRPRGVDEV ELYWTYFGYE DDSEEMTRHR LLQANLAGPG GYISMEDGEA
     VQLVHETSAR AQAQHALVEI GGTGEIKDAK NLISEVPIRG FWSYYCELMG FEAGTPRNQA
     RVVNQEAA
//
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