ID A0A0M4QXK1_9PSEU Unreviewed; 399 AA.
AC A0A0M4QXK1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Aromatic-ring-hydroxylating dioxygenase {ECO:0000313|EMBL:ALE84881.1};
GN ORFNames=XF36_18515 {ECO:0000313|EMBL:ALE84881.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE84881.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE84881.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE84881.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
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DR EMBL; CP011868; ALE84881.1; -; Genomic_DNA.
DR RefSeq; WP_060712952.1; NZ_CP011868.1.
DR AlphaFoldDB; A0A0M4QXK1; -.
DR KEGG; pseh:XF36_18515; -.
DR PATRIC; fig|1641402.3.peg.3975; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000062082; 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 GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR CDD; cd08887; RHO_alpha_C_3; 1.
DR CDD; cd03469; Rieske_RO_Alpha_N; 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; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43756:SF5; 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 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:ALE84881.1};
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:UP000062082}.
FT DOMAIN 68..175
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 45575 MW; D4F9D702A69978DF CRC64;
MSTDQTAASA QQTDELAARN DRIRRALDHI RNDSTDEYDG IASFTAEEFT DPEIARRERD
AVFGRVPSIV CHGSEIPKPN DFMTLQMPRN DVIIVRQKDH SVKAFVNLCR HRGALLEEQE
KGRCRLFSCG YHRWSYDTDG SLRAITRDNT FGEIDRSQYG LIELPAEERH GFVWMVDDAA
AEIDVASWLG AEMDGILAGY GMDKLVSAQA EGFDEPVNWK IMQDAFLDGY HIQYAHPNTA
AKHIHTNVMA AEDFGRHARF IAPRKTIDKY LEEPPAPDED LSPYVTETHF LLPNSTLLRQ
PDHFELLTFR PHPTDPGRCR MEMRLVVPKV EDSGMDSERW TKIWEKNWKI LLAVLHQEDF
PLLRSSQRGM GSANAGGMLL GRNEVINQIF HRELRKLVS
//
