ID   CRTP_STAAE              Reviewed;         497 AA.
AC   Q53589; A6QK54;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=4,4'-diaponeurosporene oxygenase {ECO:0000303|PubMed:16020541};
DE            EC=1.14.99.- {ECO:0000250|UniProtKB:Q2FV57};
DE   AltName: Full=4,4'-diaponeurosporene oxidase {ECO:0000303|PubMed:16020541};
DE   AltName: Full=Carotenoid oxidase {ECO:0000250|UniProtKB:Q2FV57};
GN   Name=crtP {ECO:0000303|PubMed:16020541}; OrderedLocusNames=NWMN_2464;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=16020541; DOI=10.1074/jbc.m505070200;
RA   Pelz A., Wieland K.-P., Putzbach K., Hentschel P., Albert K., Goetz F.;
RT   "Structure and biosynthesis of staphyloxanthin from Staphylococcus
RT   aureus.";
RL   J. Biol. Chem. 280:32493-32498(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
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:0000269|PubMed:16020541}.
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   -!- 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:0000269|PubMed:16020541}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtP subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA66626.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X97985; CAA66626.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AP009351; BAF68736.1; -; Genomic_DNA.
DR   RefSeq; WP_000160456.1; NZ_CP023390.1.
DR   AlphaFoldDB; Q53589; -.
DR   SMR; Q53589; -.
DR   EnsemblBacteria; BAF68736; BAF68736; NWMN_2464.
DR   KEGG; sae:NWMN_2464; -.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   OMA; FTMRWVF; -.
DR   UniPathway; UPA00029; UER00558.
DR   Proteomes; UP000006386; 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_0000285223"
FT   BINDING         7..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  57187 MW;  20C55EC59459ABF8 CRC64;
     MTKHIIVIGG GLGGISAAIR MAQSGYSVSL YEQNNHIGGK VNRHESDGFG FDLGPSILTM
     PYIFEKLFEY SKKQMSDYVT IKRLPHQWRS FFPDGTTIDL YEGIKETGQH NAILSKQDIE
     ELQNYLNYTR RIDRITEKGY FNYGLDTLSQ IIKFHGPLNA LINYDYVHTM QQAIDKRISN
     PYLRQMLGYF IKYVGSSSYD APAVLSMLFH MQQEQGLWYV EGGIHHLANA LEKLAREEGV
     TIHTGARVDN IKTYQRRVTG VRLDTGEFVK ADYIISNMEV IPTYKYLIHL DTQRLNKLER
     EFEPASSGYV MHLGVACQYP QLAHHNFFFT ENAYLNYQQV FHEKVLPDDP TIYLVNTNKT
     DHTQAPVGYE NIKVLPHIPY IQDQPFTTED YAKFRDKILD KLEKMGLTDL RKHIIYEDVW
     TPEDIEKNYR SNRGAIYGVV ADKKKNKGFK FPKESQYFEN LYFVGGSVNP GGGMPMVTLS
     GQQVADKINA REAKNRK