ID   CRTP_STAAB              Reviewed;         497 AA.
AC   Q2YWE5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, 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=SAB2437c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI82125.1; -; Genomic_DNA.
DR   RefSeq; WP_000160451.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWE5; -.
DR   SMR; Q2YWE5; -.
DR   KEGG; sab:SAB2437c; -.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   OMA; FTMRWVF; -.
DR   UniPathway; UPA00029; UER00558.
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_0000285224"
FT   BINDING         7..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  57214 MW;  0CDBA0146512131A CRC64;
     MTKHIIVIGG GLGGISAAIR MAQSGYSVSL YEQNNHIGGK VNRHESDGFG FDLGPSILTM
     PYIFEKLFEY SKKQMSDYVT IKRLPHQWRS FFPDGTTIDL YEGIKETGQH NAILSKKDIE
     ELQNYLNYTR RIDRITEKGY FNYGLDTLSQ IIKFHGPLNA LINYDYVHTM QQAIDKRISN
     PYLRQMLGYF IKYVGSSSYD APAVLSMLFH MQQEQGLWYV EGGIHHLANA LEKLAREEGV
     TIHTGTRVDN IKIYQRHVTG VRLDTGEFVK ADYIISNMEV IPTYKYLLHL GTQRLNKLER
     EFEPASSGYV MHLGVACQYP QLEHHNFFFT ENAYLNYQQV FHEKVLPDDP TIYLVNTNKT
     DHTQAPVGYE NIKVLPHIPY IQDQPFTTED YAKFRDKILD KLEKMGLTDL RKHIIYEDVW
     TPEDIEKNYR SNRGAIYGVV ADKKKNKGFK FTKESQYFEN LYFVGGSVNP GGGMPMVTLS
     GQQVADKINA REAKNRK