CRTP_STAAW
ID CRTP_STAAW Reviewed; 497 AA.
AC Q8NUQ3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=4,4'-diaponeurosporene oxygenase {ECO:0000250|UniProtKB:Q2FV57};
DE EC=1.14.99.- {ECO:0000250|UniProtKB:Q2FV57};
DE AltName: Full=4,4'-diaponeurosporene oxidase {ECO:0000250|UniProtKB:Q2FV57};
DE AltName: Full=Carotenoid oxidase {ECO:0000250|UniProtKB:Q2FV57};
GN Name=crtP {ECO:0000250|UniProtKB:Q2FV57}; OrderedLocusNames=MW2485;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; 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 the oxidation of the
CC terminal methyl side group of 4,4'-diaponeurosporene to form 4,4'-
CC diaponeurosporen-4-al. {ECO:0000250|UniProtKB:Q2FV57}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 AH2 + all-trans-4,4'-diaponeurosporene + 2 O2 = 4,4'-
CC diaponeurosporenal + 2 A + 3 H2O; Xref=Rhea:RHEA:56104,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:62743, ChEBI:CHEBI:79065;
CC Evidence={ECO:0000250|UniProtKB:Q2FV57};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P21685};
CC -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC staphyloxanthin from farnesyl diphosphate: step 3/5.
CC {ECO:0000250|UniProtKB:Q2FV57}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC CrtP subfamily. {ECO:0000250|UniProtKB:Q2FV57}.
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DR EMBL; BA000033; BAB96350.1; -; Genomic_DNA.
DR RefSeq; WP_000160454.1; NC_003923.1.
DR AlphaFoldDB; Q8NUQ3; -.
DR SMR; Q8NUQ3; -.
DR EnsemblBacteria; BAB96350; BAB96350; BAB96350.
DR KEGG; sam:MW2485; -.
DR HOGENOM; CLU_019722_2_1_9; -.
DR OMA; FTMRWVF; -.
DR UniPathway; UPA00029; UER00558.
DR Proteomes; UP000000418; 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..497
FT /note="4,4'-diaponeurosporene oxygenase"
FT /id="PRO_0000285229"
FT BINDING 7..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 57217 MW; 70814ED59449BBFF CRC64;
MTKHIIVIGG GLGGISAAIR MAQSGYSVSL YEQNNHIGGK VNRHESDGFG FDLGPSILTM
PYIFEKLFEY SKKQMSDYVT IKRLPHQWRS FFPDGTTIDL YEGIKETGQH NAILSKQDIE
ELQNYLNYTR RIDRITEKGY FNYGLDTLSQ IIKFHGPLNA LINYDYVHTM QQAIDKRISN
PYLRQMLGYF IKYVGSSSYD APAVLSMLFH MQQEQGLWYV EGGIHHLANA LEKLAREEGV
TIHTGARVDN IKTYQRRVTG VRLDTGEFVK ADYIISNMEV IPTYKYLIHL DTQRLNKLER
EFEPASSGYV MHLGVACQYP QLAHHNFFFT ENAYLNYQQV FHEKVLPDDP TIYLVNTNKT
DHTQAPVGYE NIKVLPHIPY IQDQPFTTED YAKFRDKILD KLEKMGLTDL RKHIIYEDVW
TPEDIEKNYR SNRGAIYGFV ADKKKNKGFK FPKESQYFEN LYFVGGSVNP GGGIPMVTLS
GQQVADKINA REAKNRK
