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Database: UniProt
Entry: E3HIK2_ACHXA
LinkDB: E3HIK2_ACHXA
Original site: E3HIK2_ACHXA 
ID   E3HIK2_ACHXA            Unreviewed;       419 AA.
AC   E3HIK2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Ring hydroxylating alpha subunit family protein 1 {ECO:0000313|EMBL:ADP14287.1};
DE            EC=1.14.12.- {ECO:0000313|EMBL:ADP14287.1};
GN   OrderedLocusNames=AXYL_00939 {ECO:0000313|EMBL:ADP14287.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP14287.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP14287.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP14287.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR   EMBL; CP002287; ADP14287.1; -; Genomic_DNA.
DR   RefSeq; WP_013391675.1; NC_014640.1.
DR   AlphaFoldDB; E3HIK2; -.
DR   STRING; 762376.AXYL_00939; -.
DR   KEGG; axy:AXYL_00939; -.
DR   PATRIC; fig|762376.5.peg.939; -.
DR   eggNOG; COG4638; Bacteria.
DR   HOGENOM; CLU_026244_4_0_4; -.
DR   OrthoDB; 9790995at2; -.
DR   Proteomes; UP000006876; 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; cd08880; RHO_alpha_C_ahdA1c-like; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR043264; AhdA1c-like_alpha_C.
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};
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:ADP14287.1}.
FT   DOMAIN          46..165
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   419 AA;  48005 MW;  99F531881E6976D7 CRC64;
     MNAPEQPIEF APRWQTDGSH RIPFGVYTDA ALHQREMERF FYRAHWSYVG LEAEIPNPGD
     FKRTAVGERS VILLRDNDGQ VRVVENVCAH RGVQFCRERS GNRSEFVCPY HQWNYDLQGN
     LIGVPFRRGV KQDGKVNGGM PPDFKPEEHG LTKLAVACRN GVVFASFDHD VEPLEDYLGP
     DILHYFDRVF DGRELVIHGY SRQRIPGNWK LMQENIKDPY HPGLLHTWFV TFGLWRADNR
     SELKMDQHLR HAAMISTRGQ GGKGSVTSGV SSFKEQMSLN DDRFLDIVPE PWWNGPTAVL
     MTLFPSVIIQ QQVNSLSTRH IQPVGHDAFD FVWTHFGFAE DAPEMTRRRL RQANLFGPAG
     FVSADDGEVI EFSQSGFEQK PWHRSVAELG GKTAENTDHM VTETLIRGMY AYWRRVMEA
//
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