ID   CRTP_STAAR              Reviewed;         497 AA.
AC   Q6GDN5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=4,4'-diaponeurosporene oxygenase {ECO:0000250|UniProtKB:Q2FV57};
DE            EC=1.14.99.- {ECO:0000250|UniProtKB:Q2FV57};
DE   AltName: Full=4,4'-diaponeurosporene oxidase {ECO:0000250|UniProtKB:Q2FV57};
DE   AltName: Full=Carotenoid oxidase {ECO:0000250|UniProtKB:Q2FV57};
GN   Name=crtP {ECO:0000250|UniProtKB:Q2FV57}; OrderedLocusNames=SAR2646;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of the yellow-orange carotenoid
CC       staphyloxanthin, which plays a role in the virulence via its protective
CC       function against oxidative stress. Catalyzes the oxidation of the
CC       terminal methyl side group of 4,4'-diaponeurosporene to form 4,4'-
CC       diaponeurosporen-4-al. {ECO:0000250|UniProtKB:Q2FV57}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 AH2 + all-trans-4,4'-diaponeurosporene + 2 O2 = 4,4'-
CC         diaponeurosporenal + 2 A + 3 H2O; Xref=Rhea:RHEA:56104,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:62743, ChEBI:CHEBI:79065;
CC         Evidence={ECO:0000250|UniProtKB:Q2FV57};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P21685};
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 3/5.
CC       {ECO:0000250|UniProtKB:Q2FV57}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtP subfamily. {ECO:0000250|UniProtKB:Q2FV57}.
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DR   EMBL; BX571856; CAG41623.1; -; Genomic_DNA.
DR   RefSeq; WP_000160442.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDN5; -.
DR   SMR; Q6GDN5; -.
DR   KEGG; sar:SAR2646; -.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   OMA; FTMRWVF; -.
DR   OrthoDB; 418913at2; -.
DR   UniPathway; UPA00029; UER00558.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02734; crtI_fam; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; FAD; Flavoprotein; Oxidoreductase; Virulence.
FT   CHAIN           1..497
FT                   /note="4,4'-diaponeurosporene oxygenase"
FT                   /id="PRO_0000285226"
FT   BINDING         7..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  57223 MW;  AB011ADF89A79733 CRC64;
     MTKHIIVIGG GLGGISAAIR MAQSGYSVSL YEQNNHIGGK VNRHESDDFG FDLGPSILTM
     PYIFEKLFEY SKKQMSDYVT IKRLPHQWRS FFPDGTTIDL YEGIKETGQH NAILSKQDIE
     ELQNYLNYTR RIDRITEKGY FNYGLDTLSQ IIKFHGPLNA LINYDYVHTM QQAIDKRISN
     PYLRQMLGYF IKYVGSSSYD APAVLSMLFH MQQEQGLWYV EGGIHHLANA LEKLAREEGV
     TIHTGTRVDN IKTYERCVTG VRLDTGEFVK ADYIISNMEV IPTYKYLLHL DTQRLNKLER
     EFEPASSGYV MHLGVACQYP QLAHHNFFFT ENAYLNYQQV FHEKVLPDDP TIYLVNTNKT
     DHTQAPVGYE NIKVLPHIPY IQDQPFTTED YAKFRDKILD KLEKMGLTDL RKHIIYEDVW
     TPEDIEKNYR SNRGAIYGVV ADKKKNKGFK FPKESQYFEN LYFVGGSVNP GGGMPMVTLS
     GQQVADKINA REAKNRK