ID   CCO_MYCTO               Reviewed;         501 AA.
AC   P9WPR4; F2GNJ3; L0T7C1; O06785; Q7D9H3;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Carotenoid cleavage oxygenase;
DE            Short=CCO;
DE            EC=1.13.11.-;
DE   AltName: Full=Carotenoid 13,14/15,15'-oxygenase;
GN   OrderedLocusNames=MT0683;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the oxidative cleavage of several carotenoids and
CC       apocarotenoids in vitro. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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; AE000516; AAK44908.1; -; Genomic_DNA.
DR   PIR; A70534; A70534.
DR   RefSeq; WP_003403360.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPR4; -.
DR   SMR; P9WPR4; -.
DR   EnsemblBacteria; AAK44908; AAK44908; MT0683.
DR   KEGG; mtc:MT0683; -.
DR   PATRIC; fig|83331.31.peg.726; -.
DR   HOGENOM; CLU_016472_0_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543; PTHR10543; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..501
FT                   /note="Carotenoid cleavage oxygenase"
FT                   /id="PRO_0000426906"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         494
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  54944 MW;  9224DE6F3E99C9DB CRC64;
     MTTAQAAESQ NPYLEGFLAP VSTEVTATDL PVTGRIPEHL DGRYLRNGPN PVAEVDPATY
     HWFTGDAMVH GVALRDGKAR WYRNRWVRTP AVCAALGEPI SARPHPRTGI IEGGPNTNVL
     THAGRTLALV EAGVVNYELT DELDTVGPCD FDGTLHGGYT AHPQRDPHTG ELHAVSYSFA
     RGHRVQYSVI GTDGHARRTV DIEVAGSPMM HSFSLTDNYV VIYDLPVTFD PMQVVPASVP
     RWLQRPARLV IQSVLGRVRI PDPIAALGNR MQGHSDRLPY AWNPSYPARV GVMPREGGNE
     DVRWFDIEPC YVYHPLNAYS ECRNGAEVLV LDVVRYSRMF DRDRRGPGGD SRPSLDRWTI
     NLATGAVTAE CRDDRAQEFP RINETLVGGP HRFAYTVGIE GGFLVGAGAA LSTPLYKQDC
     VTGSSTVASL DPDLLIGEMV FVPNPSARAE DDGILMGYGW HRGRDEGQLL LLDAQTLESI
     ATVHLPQRVP MGFHGNWAPT T