ID   CRTN_STAHJ              Reviewed;         501 AA.
AC   Q4L975;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 118.
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=SH0491;
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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE03800.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AP006716; BAE03800.1; ALT_FRAME; Genomic_DNA.
DR   STRING; 279808.SH0491; -.
DR   PRIDE; Q4L975; -.
DR   EnsemblBacteria; BAE03800; BAE03800; SH0491.
DR   KEGG; sha:SH0491; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_019722_2_1_9; -.
DR   UniPathway; UPA00029; UER00557.
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..501
FT                   /note="4,4'-diapophytoene desaturase (4,4'-
FT                   diaponeurosporene-forming)"
FT                   /id="PRO_0000272199"
FT   BINDING         5..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  56542 MW;  6AEE9161F1CAAE3C CRC64;
     MXIAVVGAGV TGLAAAARLA AKGHQVTIFE KNEQVGGRMS QFKKDGFTFD MGPTIVMVPD
     VYKAVFEESG KRFEDYVDMK PLTHIFDIYF SDKDKVSVST DLAQLSQTLE ATEPGSTQGF
     MQFLTDVYKR YEVARKYFLE RTFRKPSEFY NPLTLYRGLK LKTFNNANQL IDNYVSNEKI
     RKLLAFQTLY IGIDPKQGPS IYSIIPMIEM VHGVHYIKGG MYGLAQGLLQ LGQDHGVKVE
     LNADVQEIII DPKFKRADGL RVNGDIRRFD KVLCTADFPY VAQNLMPVHS PLKNYSPEKV
     DNMDYSCSAF LIYAGINRQL RDKLHVHNVV FARDFRGNID DIFSGKMPDD PSLYLYFPSV
     EDEALAPKDQ TGMYVLMPVP ELKTGEIDWN DPNMVEKAKD VIYNKLETIE ALKDIRQDVV
     SETVFTPLDF ESRYNAKFGS AFGLMPTLTQ SNYYRPPNVS RDYKDLYFAG ASTHPGAGVP
     IVLTSAKITA EAMLEDIEHG K