ID   CRTN_STAAC              Reviewed;         502 AA.
AC   Q5HCY9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SACOL2576;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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 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; CP000046; AAW38578.1; -; Genomic_DNA.
DR   RefSeq; WP_000686163.1; NC_002951.2.
DR   AlphaFoldDB; Q5HCY9; -.
DR   SMR; Q5HCY9; -.
DR   EnsemblBacteria; AAW38578; AAW38578; SACOL2576.
DR   KEGG; sac:SACOL2576; -.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   OMA; INYPKGG; -.
DR   UniPathway; UPA00029; UER00557.
DR   Proteomes; UP000000530; 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'-diapophytoene desaturase (4,4'-
FT                   diaponeurosporene-forming)"
FT                   /id="PRO_0000272193"
FT   BINDING         5..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   502 AA;  56689 MW;  9A1A24A5F436AE8C CRC64;
     MKIAVIGAGV TGLAAAARIA SQGHEVTIFE KNNNVGGCMN QLKKDGFTFD MGPTIVMMPD
     VYKDVFTACG KNYEDYIELR QLRYIYDVYF DHDDRITVPT DLAELQQMLE 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 VDEMIKDIER GV