P17054 (CRTI_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phytoene desaturase (neurosporene-forming)
EC=1.3.99.28

Alternative name(s):
3-step phytoene desaturase
Phytoene dehydrogenase

Gene names

Name:	crtI
Ordered Locus Names:	RCAP_rcc00679

Organism

Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]

Taxonomic identifier

272942 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter › Rhodobacter capsulatus

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts phytoene into all-trans-neurosporene as the major product, via the intermediary of phytofluene and zeta-carotene, by the introduction of three double bonds. Both intermediates, phytofluene and zeta-carotene, can be used as substrates and converted to neurosporene. 1,2-epoxy phytoene is also a suitable substrate whereas the C30 diapophytoene is not. Ref.6
Catalytic activity	15-cis-phytoene + 3 acceptor = all-trans-neurosporene + 3 reduced acceptor. Ref.6
Cofactor	FAD. Ref.6
Enzyme regulation	Is inhibited by diphenylamine (DPA). Is also slightly inhibited by NAD, NADP or ATP in the presence of FAD. Ref.6
Pathway	Carotenoid biosynthesis.
Sequence similarities	Belongs to the carotenoid/retinoid oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM=33.3 µM for phytoene Ref.6 KM=16.6 µM for zeta-carotene KM=4.9 µM for FAD Vmax=0.169 nmol/h/mg enzyme with phytoene as substrate Vmax=0.086 nmol/h/mg enzyme with zeta-carotene as substrate

Ontologies

Keywords
Biological process	Carotenoid biosynthesis
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	carotene biosynthetic process Inferred from direct assay Ref.6. Source: UniProtKB carotenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	FAD binding Inferred from direct assay Ref.6. Source: UniProtKB oxidoreductase activity, acting on the CH-CH group of donors Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 524	524	Phytoene desaturase (neurosporene-forming)		PRO_0000067690
Regions
	Nucleotide binding	12 – 45	34	FAD Potential

Sequences

	Sequence		Length	Mass (Da)
	P17054 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 6425A7E5A06AA6B9	FASTA	524	57,978
	10 20 30 40 50 60 MSKNTEGMGR AVVIGAGLGG LAAAMRLGAK GYKVTVVDRL DRPGGRGSSI TKGGHRFDLG 70 80 90 100 110 120 PTIVTVPDRL RELWADCGRD FDKDVSLVPM EPFYTIDFPD GEKYTAYGDD AKVKAEVARI 130 140 150 160 170 180 SPGDVEGFRH FMWDAKARYE FGYENLGRKP MSKLWDLIKV LPTFGWLRAD RSVYGHAKKM 190 200 210 220 230 240 VKDDHLRFAL SFHPLFIGGD PFHVTSMYIL VSQLEKKFGV HYAIGGVQAI ADAMAKVITD 250 260 270 280 290 300 QGGEMRLNTE VDEILVSRDG KATGIRLMDG TELPAQVVVS NADAGHTYKR LLRNRDRWRW 310 320 330 340 350 360 TDEKLDKKRW SMGLFVWYFG TKGTAKMWKD VGHHTVVVGP RYKEHVQDIF IKGELAEDMS 370 380 390 400 410 420 LYVHRPSVTD PTAAPKGDDT FYVLSPVPNL GFDNGVDWSV EAEKYKAKVL KVIEERLLPG 430 440 450 460 470 480 VAEKITEEVV FTPETFRDRY LSPLGAGFSL EPRILQSAWF RPHNASEEVD GLYLVGAGTH 490 500 510 520 PGAGVPSVIG SGELVAQMIP DAPKPETPAA AAPKARTPRA KAAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence, organization, and nature of the protein products of the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus." Armstrong G.A., Alberti M., Leach F., Hearst J.E. Mol. Gen. Genet. 216:254-268(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[2]	"Carotenoid biosynthesis in photosynthetic bacteria. Genetic characterization of the Rhodobacter capsulatus CrtI protein." Bartley G.E., Scolnik P.A. J. Biol. Chem. 264:13109-13113(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[3]	Erratum Bartley G.E., Scolnik P.A. J. Biol. Chem. 264:18260-18260(1989)
[4]	"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003." Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R. J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[5]	"Carotenoid desaturases from Rhodobacter capsulatus and Neurospora crassa are structurally and functionally conserved and contain domains homologous to flavoprotein disulfide oxidoreductases." Bartley G.E., Schmidhauser T.J., Yanofsky C., Scolnik P.A. J. Biol. Chem. 265:16020-16024(1990) [PubMed] [Europe PMC] [Abstract] Cited for: SIMILARITY TO CAROTENOID DESATURASES.
[6]	"Purification in an active state and properties of the 3-step phytoene desaturase from Rhodobacter capsulatus overexpressed in Escherichia coli." Raisig A., Bartley G., Scolnik P., Sandmann G. J. Biochem. 119:559-564(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, KINETIC PARAMETERS, ENZYME REGULATION. Strain: ATCC BAA-309 / NBRC 16581 / SB1003.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52291 Genomic DNA. Translation: CAA36533.1. Z11165 Genomic DNA. Translation: CAA77540.1. J04969 Genomic DNA. Translation: AAA50313.1. CP001312 Genomic DNA. Translation: ADE84444.1.
PIR	A32617.
RefSeq	YP_003576851.1. NC_014034.1.
3D structure databases
ProteinModelPortal	P17054.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADE84444; ADE84444; RCAP_rcc00679.
GeneID	9003508.
KEGG	rcp:RCAP_rcc00679.
PATRIC	35501426. VBIRhoCap134200_0690.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000278176.
KO	K10027.
OMA	GPRYRES.
ProtClustDB	CLSK940830.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14931. RCAP272942:GJIY-692-MONOMER.
Family and domain databases
InterPro	IPR002937. Amino_oxidase. IPR014105. CrtI_fam. IPR008150. Phytoene_DH_bac_CS. [Graphical view]
PANTHER	PTHR10668:SF3. PTHR10668:SF3. 1 hit.
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
TIGRFAMs	TIGR02734. crtI_fam. 1 hit.
PROSITE	PS00982. PHYTOENE_DH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CRTI_RHOCB

Accession

Primary (citable) accession number: P17054
Secondary accession number(s): D5AP72

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program