CRTN_STAAS
ID CRTN_STAAS Reviewed; 502 AA.
AC Q6G6B3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SAS2447;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571857; CAG44263.1; -; Genomic_DNA.
DR RefSeq; WP_000686167.1; NC_002953.3.
DR AlphaFoldDB; Q6G6B3; -.
DR SMR; Q6G6B3; -.
DR KEGG; sas:SAS2447; -.
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_0000272197"
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