ID   CRTN_STAAB              Reviewed;         502 AA.
AC   Q2YWE8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=4,4'-diapophytoene desaturase (4,4'-diaponeurosporene-forming) {ECO:0000250|UniProtKB:O07855};
DE            EC=1.3.8.- {ECO:0000250|UniProtKB:O07855};
DE   AltName: Full=Dehydrosqualene desaturase {ECO:0000250|UniProtKB:O07855};
GN   Name=crtN {ECO:0000250|UniProtKB:O07855}; OrderedLocusNames=SAB2434c;
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 three successive
CC       dehydrogenation reactions that lead to the introduction of three double
CC       bonds into 4,4'-diapophytoene (dehydrosqualene), with 4,4'-
CC       diapophytofluene and 4,4'-diapo-zeta-carotene as intermediates, and
CC       4,4'-diaponeurosporene (the major deep-yellow pigment in staphylococci
CC       strains) as the end product. {ECO:0000250|UniProtKB:O07855}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-cis-4,4'-diapophytoene + 3 FAD + 3 H(+) = all-trans-4,4'-
CC         diaponeurosporene + 3 FADH2; Xref=Rhea:RHEA:42800, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62738,
CC         ChEBI:CHEBI:62743; Evidence={ECO:0000250|UniProtKB:O07855};
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 2/5.
CC       {ECO:0000250|UniProtKB:O07855}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       CrtN subfamily. {ECO:0000305}.
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DR   EMBL; AJ938182; CAI82122.1; -; Genomic_DNA.
DR   RefSeq; WP_000686193.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWE8; -.
DR   SMR; Q2YWE8; -.
DR   KEGG; sab:SAB2434c; -.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   OMA; INYPKGG; -.
DR   UniPathway; UPA00029; UER00557.
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'-diapophytoene desaturase (4,4'-
FT                   diaponeurosporene-forming)"
FT                   /id="PRO_0000272192"
FT   BINDING         5..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   502 AA;  56775 MW;  9894C597C5FFA2ED CRC64;
     MKIAVIGAGV TGLAAAARIA SQGHEVTIFE KNTNVGGRMN QLKKDGFTFD MGPTIVMMPD
     VYKDVFTMCG KNYEDYIELR QLRYIYDVYF DRDDRITVPT DLAELQHMLE SIEPGSTHGF
     MSFLTDVYKK YEIARRYFLE RTYRKPSDFY NMTSLVQGAK LKTLNHADQL IEHYIDNEKI
     QKLLAFQTLY IGIDPKRGPS LYSIIPMIEM MFGVHFIKGG MYGMAQGLAQ LNKDLGVNIE
     LNAEIEQIII DPKFKRADAI KVNGDIRKFD KILCTADFPS VAESLMPDFA PIKKYPPHKI
     ADLDYSCSAF LMYIGIDIDV TDQVRLHNVI FSDDFRGNIE EIFEGRLSYD PSIYVYVPAV
     ADKSLAPEGK TGIYVLMPTP ELKTGSGIDW SDEALTQQIK EIIYRKLATI EVFEDIKSHI
     VSETIFTPND FEQTYHAKFG SAFGLMPTLA QSNYYRPQNV SRDYKDLYFA GASTHPGAGV
     PIVLTSAKIT VDEMVKDIEQ GV