CRTP_STAAN
ID CRTP_STAAN Reviewed; 497 AA.
AC Q7A3D9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SA2351;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB43655.1; -; Genomic_DNA.
DR PIR; E90061; E90061.
DR RefSeq; WP_000160471.1; NC_002745.2.
DR AlphaFoldDB; Q7A3D9; -.
DR SMR; Q7A3D9; -.
DR EnsemblBacteria; BAB43655; BAB43655; BAB43655.
DR KEGG; sau:SA2351; -.
DR HOGENOM; CLU_019722_2_1_9; -.
DR OMA; FTMRWVF; -.
DR UniPathway; UPA00029; UER00558.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW Carotenoid biosynthesis; FAD; Flavoprotein; Oxidoreductase; Virulence.
FT CHAIN 1..497
FT /note="4,4'-diaponeurosporene oxygenase"
FT /id="PRO_0000285230"
FT BINDING 7..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 57174 MW; E20EB9DDF5141C9D CRC64;
MTKHIIVIGG GLGGISAAIR MAQSGYSVSL YEQNTHIGGK 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 SNRGAIYGVV ADKKKNKGFK FPKESQYFEN LYFVGGSVNP GGGMPMVTLS
GQQVADKINA REAKNRK