ID H0E5L2_9ACTN Unreviewed; 442 AA.
AC H0E5L2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Putative dioxygenase hydroxylase component {ECO:0000313|EMBL:EHN11047.1};
GN ORFNames=PAI11_21070 {ECO:0000313|EMBL:EHN11047.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN11047.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN11047.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN11047.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
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:EHN11047.1}.
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DR EMBL; AGUD01000191; EHN11047.1; -; Genomic_DNA.
DR RefSeq; WP_007574649.1; NZ_AGUD01000191.1.
DR AlphaFoldDB; H0E5L2; -.
DR PATRIC; fig|1097667.3.peg.2089; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000005143; 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: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; 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:EHN11047.1};
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:UP000005143}.
FT DOMAIN 45..124
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 442 AA; 49120 MW; D2820B689925C308 CRC64;
MTPTTVPADS AAWDALIEPD RVHGSLYTDP AIFDAEMERI WYRTWVYVGH ESEVPQPNDY
VVKSIGPQPI IMSRDKQGEI HLLLNRCTHR ANLVCDAAKG NSSAFRCPYH GWTFSNTGKL
LGYPFNSGYG GTEEKRNLGL GRVARVASYQ GFVFGSFAEE GPTLEEHLGG ATDAFDRLVE
LSPTGKLDIS AGWLQHEAKA NWKMLVENET DGYHPQFVHA SIFSVAKSGI GDLYGEKSTA
VSRDLGGGHT ENDLRPEFRR IDEPMGWFGT TADRLPEYVE HLQAARGPER AREIMIDGAP
HVMVYPNLFI AEIQLFVIQP LAVDRTVQHV TAIQYEGEPQ LNRRMLQQTI GSVGPAGLLL
ADDTEMYERN QRGVHARTPE WLVLKRGTHR ERRDGDGFTI GDATDEVPQR AIWRHYRELM
EAGDGDGAVA PPAVPTANGS VR
//
