ID A0A1X1ZIW3_9MYCO Unreviewed; 423 AA.
AC A0A1X1ZIW3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ring-hydroxylating oxygenase subunit alpha {ECO:0000313|EMBL:ORW23252.1};
GN ORFNames=AWC19_11875 {ECO:0000313|EMBL:ORW23252.1};
OS Mycobacterium palustre.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=153971 {ECO:0000313|EMBL:ORW23252.1, ECO:0000313|Proteomes:UP000193529};
RN [1] {ECO:0000313|EMBL:ORW23252.1, ECO:0000313|Proteomes:UP000193529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44572 {ECO:0000313|EMBL:ORW23252.1,
RC ECO:0000313|Proteomes:UP000193529};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
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:ORW23252.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQPJ01000109; ORW23252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1ZIW3; -.
DR STRING; 153971.AWC19_11875; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000193529; 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};
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 47..145
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 423 AA; 47735 MW; ABEEF3FB99E0D41F CRC64;
MTSLIEPAAT TRSGYDHLIR RDKVHGSMYT DPAIFVEELR RIWYRTWVFI GHESEVPQPN
DYVRKRLGLQ DVILTRDRDG ELHLLLNRCA HRGNQICDEG QGNSSTFRCP YHGWTFRNTG
ELVGFPFFKG YGQRKLELNL GRVPRVDTYQ GFVFASFAAD GPGLVDHLGA AAGEIDRLVR
LSPEGKVQLT AGWLQHQTRA NWKLLVENET DGYHPQFVHG SIFGVTGSPI GALYSDTSTA
VTRDLGQGHS ENDLRPEFRK FAEPMRWFGT TEARVPEYVA AMRKRYGEDA EKIMIEGAPH
VMIFPNLFIA EIQVFNIQPV AVGECIQYST AIQMAGAPEL NQRMVSQCMG SVGPAGMLLA
DDTEMYERNQ LGLECLTPEW LDIRRGLNRE RVDENGFTVG GATDETGMRS FWSRYKTLME
AES
//