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Database: UniProt
Entry: V5XCI4_MYCNE
LinkDB: V5XCI4_MYCNE
Original site: V5XCI4_MYCNE 
ID   V5XCI4_MYCNE            Unreviewed;       442 AA.
AC   V5XCI4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=p-cumate dioxygenase large subunit (CmtAb) {ECO:0000313|EMBL:AHC26140.1};
GN   ORFNames=D174_16905 {ECO:0000313|EMBL:AHC26140.1};
OS   Mycolicibacterium neoaurum VKM Ac-1815D.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC26140.1, ECO:0000313|Proteomes:UP000018763};
RN   [1] {ECO:0000313|EMBL:AHC26140.1, ECO:0000313|Proteomes:UP000018763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC26140.1,
RC   ECO:0000313|Proteomes:UP000018763};
RX   PubMed=24435872;
RA   Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA   Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT   Strain VKM Ac-1815D.";
RL   Genome Announc. 2:e01177-13(2014).
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}.
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DR   EMBL; CP006936; AHC26140.1; -; Genomic_DNA.
DR   RefSeq; WP_019509762.1; NC_023036.2.
DR   AlphaFoldDB; V5XCI4; -.
DR   KEGG; mne:D174_16905; -.
DR   eggNOG; COG4638; Bacteria.
DR   HOGENOM; CLU_026244_4_0_11; -.
DR   Proteomes; UP000018763; 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; cd08879; RHO_alpha_C_AntDO-like; 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: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:AHC26140.1};
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:UP000018763}.
FT   DOMAIN          40..147
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          413..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  49910 MW;  FC9CB4DE90DC751D CRC64;
     MSEYVVDDRE MPCFRVARQT MVDPTILERE RTLIFDKSWL YVGHESELAK PNSFKTRTLA
     GRPVIFTRDS RGQIRVWLNS CPHRGAMICR EREGNARFHT CFYHGWSFNT AGEQVSTPGD
     ESYGPNFDRP GLAKPPRLES YRGFVFASFD PDIVDLETYL AGAKEYLDLV ADQSDMGMQV
     LEGTHEYSCK ANWKLLVENS FDGYHAMTTH QRYFAMVIAA RGSIDTSLII GKDRGIDLGN
     GHAVIAAGPG GDQILGRPLS AAGQAERDAR YAAIGEKYGT EWATRLRGQR NLVIFPNLVI
     IDLVMGVLIR KIDPITPDYM EVTAWHIVPP EEGAELRAQR LDNFLTFWGP SGLATPDDVE
     ALESAQRAFA TRKELPWSDI SRGMSSRVNT SQDELQMRTW WRQWNRLITG EVLPDEEKDP
     MGLPWSGRRR EPTVSHLPTP AP
//
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