CRTI_RHOCB
ID CRTI_RHOCB Reviewed; 524 AA.
AC P17054; D5AP72;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phytoene desaturase (neurosporene-forming);
DE EC=1.3.99.28;
DE AltName: Full=3-step phytoene desaturase;
DE AltName: Full=Phytoene dehydrogenase;
GN Name=crtI; OrderedLocusNames=RCAP_rcc00679;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2747617; DOI=10.1007/bf00334364;
RA Armstrong G.A., Alberti M., Leach F., Hearst J.E.;
RT "Nucleotide sequence, organization, and nature of the protein products of
RT the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus.";
RL Mol. Gen. Genet. 216:254-268(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2546948; DOI=10.1016/s0021-9258(18)51602-1;
RA Bartley G.E., Scolnik P.A.;
RT "Carotenoid biosynthesis in photosynthetic bacteria. Genetic
RT characterization of the Rhodobacter capsulatus CrtI protein.";
RL J. Biol. Chem. 264:13109-13113(1989).
RN [3]
RP ERRATUM OF PUBMED:2546948.
RA Bartley G.E., Scolnik P.A.;
RL J. Biol. Chem. 264:18260-18260(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [5]
RP SIMILARITY TO CAROTENOID DESATURASES.
RX PubMed=2144293; DOI=10.1016/s0021-9258(18)55500-9;
RA Bartley G.E., Schmidhauser T.J., Yanofsky C., Scolnik P.A.;
RT "Carotenoid desaturases from Rhodobacter capsulatus and Neurospora crassa
RT are structurally and functionally conserved and contain domains homologous
RT to flavoprotein disulfide oxidoreductases.";
RL J. Biol. Chem. 265:16020-16024(1990).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC
RP PARAMETERS, AND ACTIVITY REGULATION.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8830054; DOI=10.1093/oxfordjournals.jbchem.a021278;
RA Raisig A., Bartley G., Scolnik P., Sandmann G.;
RT "Purification in an active state and properties of the 3-step phytoene
RT desaturase from Rhodobacter capsulatus overexpressed in Escherichia coli.";
RL J. Biochem. 119:559-564(1996).
CC -!- FUNCTION: Converts phytoene into all-trans-neurosporene as the major
CC product, via the intermediary of phytofluene and zeta-carotene, by the
CC introduction of three double bonds. Both intermediates, phytofluene and
CC zeta-carotene, can be used as substrates and converted to neurosporene.
CC 1,2-epoxy phytoene is also a suitable substrate whereas the C30
CC diapophytoene is not. {ECO:0000269|PubMed:8830054}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-cis-phytoene + 3 A = 3 AH2 + all-trans-neurosporene;
CC Xref=Rhea:RHEA:30599, ChEBI:CHEBI:13193, ChEBI:CHEBI:16833,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:27787; EC=1.3.99.28;
CC Evidence={ECO:0000269|PubMed:8830054};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8830054};
CC -!- ACTIVITY REGULATION: Is inhibited by diphenylamine (DPA). Is also
CC slightly inhibited by NAD, NADP or ATP in the presence of FAD.
CC {ECO:0000269|PubMed:8830054}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.3 uM for phytoene {ECO:0000269|PubMed:8830054};
CC KM=16.6 uM for zeta-carotene {ECO:0000269|PubMed:8830054};
CC KM=4.9 uM for FAD {ECO:0000269|PubMed:8830054};
CC Vmax=0.169 nmol/h/mg enzyme with phytoene as substrate
CC {ECO:0000269|PubMed:8830054};
CC Vmax=0.086 nmol/h/mg enzyme with zeta-carotene as substrate
CC {ECO:0000269|PubMed:8830054};
CC -!- PATHWAY: Carotenoid biosynthesis.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; X52291; CAA36533.1; -; Genomic_DNA.
DR EMBL; Z11165; CAA77540.1; -; Genomic_DNA.
DR EMBL; J04969; AAA50313.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84444.1; -; Genomic_DNA.
DR PIR; A32617; A32617.
DR RefSeq; WP_013066423.1; NC_014034.1.
DR AlphaFoldDB; P17054; -.
DR SMR; P17054; -.
DR STRING; 272942.RCAP_rcc00679; -.
DR EnsemblBacteria; ADE84444; ADE84444; RCAP_rcc00679.
DR GeneID; 31489625; -.
DR KEGG; rcp:RCAP_rcc00679; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019722_2_1_5; -.
DR OMA; INYPKGG; -.
DR OrthoDB; 418913at2; -.
DR BioCyc; MetaCyc:MON-14931; -.
DR BRENDA; 1.3.99.28; 5381.
DR SABIO-RK; P17054; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
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 InterPro; IPR008150; Phytoene_DH_bac_CS.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02734; crtI_fam; 1.
DR PROSITE; PS00982; PHYTOENE_DH; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..524
FT /note="Phytoene desaturase (neurosporene-forming)"
FT /id="PRO_0000067690"
FT REGION 500..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 524 AA; 57978 MW; 6425A7E5A06AA6B9 CRC64;
MSKNTEGMGR AVVIGAGLGG LAAAMRLGAK GYKVTVVDRL DRPGGRGSSI TKGGHRFDLG
PTIVTVPDRL RELWADCGRD FDKDVSLVPM EPFYTIDFPD GEKYTAYGDD AKVKAEVARI
SPGDVEGFRH FMWDAKARYE FGYENLGRKP MSKLWDLIKV LPTFGWLRAD RSVYGHAKKM
VKDDHLRFAL SFHPLFIGGD PFHVTSMYIL VSQLEKKFGV HYAIGGVQAI ADAMAKVITD
QGGEMRLNTE VDEILVSRDG KATGIRLMDG TELPAQVVVS NADAGHTYKR LLRNRDRWRW
TDEKLDKKRW SMGLFVWYFG TKGTAKMWKD VGHHTVVVGP RYKEHVQDIF IKGELAEDMS
LYVHRPSVTD PTAAPKGDDT FYVLSPVPNL GFDNGVDWSV EAEKYKAKVL KVIEERLLPG
VAEKITEEVV FTPETFRDRY LSPLGAGFSL EPRILQSAWF RPHNASEEVD GLYLVGAGTH
PGAGVPSVIG SGELVAQMIP DAPKPETPAA AAPKARTPRA KAAQ
