CCO_MYCTU
ID CCO_MYCTU Reviewed; 501 AA.
AC P9WPR5; 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 34.
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=Rv0654;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND KINETIC
RP PARAMETERS.
RX PubMed=20929460; DOI=10.1111/j.1742-4658.2010.07873.x;
RA Scherzinger D., Scheffer E., Bar C., Ernst H., Al-Babili S.;
RT "The Mycobacterium tuberculosis ORF Rv0654 encodes a carotenoid oxygenase
RT mediating central and excentric cleavage of conventional and aromatic
RT carotenoids.";
RL FEBS J. 277:4662-4673(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the oxidative cleavage of several carotenoids and
CC apocarotenoids in vitro. In contrast to other carotenoid oxygenases,
CC cleaves substrates at two different sites, namely the central C15-C15'
CC and an excentric double bond at the C13-C14 position, leading to
CC retinal (C20), beta-apo-14'-carotenal (C22) and beta-apo-13-carotenone
CC (C18) from beta-carotene (C40), as well as the corresponding
CC hydroxylated products from zeaxanthin and lutein. Converts beta-apo-
CC 10'-carotenal (C27) into beta-apo-13-carotenone (C18) and to minor
CC amounts of beta-apo-15-carotenal (retinal; C20) from the cleavage at
CC the C13-C14 and the C15-C15' double bonds, respectively. Can also
CC cleave beta-apo-8'-carotenal, 3-OH-beta-apo-8'-carotenal and 3-OH-beta-
CC apo-10'-carotenal. Does not use as substrates beta-apocarotenoids that
CC have a chain length shorter than C25. Also cleaves lycopene into apo-
CC 13-lycopenone (C18) and apo-15'-lycopenal (acycloretinal, C20).
CC Moreover, is able to cleave 3,3'-dihydroxy-isorenieratene representing
CC aromatic carotenoids synthesized by other mycobacteria. Might be
CC involved in the utilization of carotenoids from host cells to produce
CC compounds required for normal growth. {ECO:0000269|PubMed:20929460}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.15 uM for beta-apo-8'-carotenal {ECO:0000269|PubMed:20929460};
CC KM=29.4 uM for beta-apo-10'-carotenal {ECO:0000269|PubMed:20929460};
CC KM=21.9 uM for 3-OH-beta-apo-8'-carotenal
CC {ECO:0000269|PubMed:20929460};
CC KM=43.8 uM for 3-OH-beta-apo-10'-carotenal
CC {ECO:0000269|PubMed:20929460};
CC Note=kcat is 393, 562, 1307 and 764 sec(-1) with beta-apo-8'-
CC carotenal, beta-apo-10'-carotenal, 3-OH-beta-apo-8'-carotenal and 3-
CC OH-beta-apo-10'-carotenal as substrate, respectively.;
CC -!- MISCELLANEOUS: M.tuberculosis is assumed to be unable to synthesize
CC conventional colored carotenoids, but the data obtained in
CC PubMed:20929460 reveal that M.tuberculosis may utilize carotenoids from
CC host cells and interfere with their retinoid metabolism. The occurrence
CC of suitable carotenoid-substrates (i.e. beta-carotene, lutein,
CC zeaxanthin and lycopene) have been shown in human plasma and tissues,
CC and the apocarotenoid substrate beta-apo-10'-carotenal may also be
CC present in lungs.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43397.1; -; Genomic_DNA.
DR PIR; A70534; A70534.
DR RefSeq; NP_215168.1; NC_000962.3.
DR RefSeq; WP_003403360.1; NZ_NVQJ01000007.1.
DR AlphaFoldDB; P9WPR5; -.
DR SMR; P9WPR5; -.
DR STRING; 83332.Rv0654; -.
DR PaxDb; P9WPR5; -.
DR DNASU; 888089; -.
DR GeneID; 888089; -.
DR KEGG; mtu:Rv0654; -.
DR TubercuList; Rv0654; -.
DR eggNOG; COG3670; Bacteria.
DR OMA; HHIPYGL; -.
DR PhylomeDB; P9WPR5; -.
DR BRENDA; 1.13.11.65; 3445.
DR BRENDA; 1.13.11.75; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0010436; F:carotenoid dioxygenase activity; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; IBA:GO_Central.
DR GO; GO:0016118; P:carotenoid catabolic process; IDA:MTBBASE.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..501
FT /note="Carotenoid cleavage oxygenase"
FT /id="PRO_0000420620"
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
