ID   CRTP_STAHJ              Reviewed;         502 AA.
AC   Q4L978;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=SH0488;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE03797.1; -; Genomic_DNA.
DR   RefSeq; WP_011274813.1; NC_007168.1.
DR   AlphaFoldDB; Q4L978; -.
DR   SMR; Q4L978; -.
DR   STRING; 279808.SH0488; -.
DR   EnsemblBacteria; BAE03797; BAE03797; SH0488.
DR   KEGG; sha:SH0488; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   OMA; FTMRWVF; -.
DR   OrthoDB; 418913at2; -.
DR   UniPathway; UPA00029; UER00558.
DR   Proteomes; UP000000543; 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..502
FT                   /note="4,4'-diaponeurosporene oxygenase"
FT                   /id="PRO_0000285233"
FT   BINDING         8..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   502 AA;  57296 MW;  DDB1EFCF86FCD56C CRC64;
     MSQKKIIIIG GGLGGISAAI RLAQSGFDVS LYDKNNHIGG KVNRLETEGF GFDLGPSILT
     MPYIFENLFN YSDKQMKDYV TIERLPLQWR SFFTNGEVID LYEDLSQMLN ANTYLTNDDI
     QQLHQFLNYA EKIHRFTEKG YFALGLDKVS EIIKYQGLLR SLKGVDYFST MQQAINRYIE
     KQKLRDMLGY FIKYVGSSSY DAPAVLTLLI HMQYEQGLWY VKGGIHKLAQ ALEQLAIEEG
     VAIHTGMDVC SIDTYFNHIT GVRLDDGSHV SADYIVSNRE VIPTYRDLLH FSNKKIAQLE
     KVYEPAASGY VMHLGVDKEY AQLAHHNFLF SNDSKRNYRE VFHDKVLPQD PTIYLVNSNK
     SDPTQAPEGH ENLKVLPHIP YIQNQPFTEE QYSDFRERVL DKLEKMGLTD LRQHIIYEDI
     WTPHDIERTY GSNKGAIYGV VADKKKNKGF KFPKQSEYFD NLFFVGGSVN PGGGMPMVTL
     SGQQVADKIN ALECKVTTDS RE