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Database: UniProt
Entry: CRTN_STAAW
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Original site: CRTN_STAAW 
ID   CRTN_STAAW              Reviewed;         502 AA.
AC   Q8NUQ6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=MW2482;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB96347.1; -; Genomic_DNA.
DR   PIR; B55548; B55548.
DR   RefSeq; WP_000686167.1; NC_003923.1.
DR   AlphaFoldDB; Q8NUQ6; -.
DR   SMR; Q8NUQ6; -.
DR   BindingDB; Q8NUQ6; -.
DR   ChEMBL; CHEMBL3832958; -.
DR   KEGG; sam:MW2482; -.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   BRENDA; 1.14.99.44; 3352.
DR   UniPathway; UPA00029; UER00557.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0140868; F:4,4'-diapophytoene desaturase (4,4'-diapolycopene-forming); IEA:RHEA.
DR   GO; GO:0102223; F:4,4'-diapophytoene desaturase (4,4'-diaponeurosporene-forming); IEA:RHEA.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   NCBIfam; TIGR02734; crtI_fam; 1.
DR   PANTHER; PTHR43734; PHYTOENE DESATURASE; 1.
DR   PANTHER; PTHR43734:SF1; PHYTOENE DESATURASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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_0000272198"
FT   BINDING         5..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   502 AA;  56714 MW;  969529997B394203 CRC64;
     MKIAVIGAGV TGLAAAARIA SQGHEVTIFE KNNNVGGRMN 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 VDEMIKDIEQ GV
//
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