Coenzyme A biosynthesis protein 3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P36076 (CAB3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Coenzyme A biosynthesis protein 3

Gene names

Name:	CAB3
Ordered Locus Names:	YKL088W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	571 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Ref.10 Ref.11
Subunit structure	Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) complex, a heterotrimer composed of CAB3, HAL3 and VHS3.
Subcellular location	Cytoplasm Ref.3.
Miscellaneous	Present with 2940 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the HFCD (homooligomeric flavin containing Cys decarboxylase) superfamily.

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	coenzyme A biosynthetic process Inferred from genetic interaction Ref.10. Source: SGD response to salt stress Inferred from genetic interaction PubMed 8923737. Source: SGD
Cellular_component	phosphopantothenoylcysteine decarboxylase complex Inferred from direct assay Ref.11. Source: SGD
Molecular_function	phosphopantothenoylcysteine decarboxylase activity Inferred from sequence or structural similarity PubMed 10592175 PubMed 14690591. Source: SGD purine nucleotide binding Inferred from sequence or structural similarity PubMed 7705654. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
PPZ1	P26570	6	EBI-26778,EBI-13807
PPZ2	P33329	4	EBI-26778,EBI-13815
SIS2	P36024	3	EBI-26778,EBI-17250
VHS3	Q08438	4	EBI-26778,EBI-30482

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 571

571

Coenzyme A biosynthesis protein 3

PRO_0000182039

Regions

Compositional bias

508 – 570

Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue

Phosphoserine Ref.6 Ref.7 Ref.9

Modified residue

116

Phosphoserine Ref.5 Ref.6 Ref.8 Ref.9

Modified residue

118

Phosphoserine Ref.8 Ref.9

Modified residue

121

Phosphoserine Ref.6

Modified residue

124

Phosphoserine Ref.6

Modified residue

230

Phosphothreonine Ref.8

Modified residue

231

Phosphoserine Ref.8

Modified residue

233

Phosphoserine Ref.9

Modified residue

239

Phosphoserine Ref.8

Modified residue

264

Phosphoserine Ref.9

Experimental info

Mutagenesis

478

C → S: Abolishes PPCDC activity. Ref.11

Sequences

Sequence

Length

Mass (Da)

Tools

P36076 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 9C674C2394EFCEAB
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FASTA

571

65,238

        10         20         30         40         50         60 
MTDEKVNSDQ NMNGKQGVNL ISSLPTTQVP VSILTNKERR KSIHDESNFE RSDSHEDQSK 

        70         80         90        100        110        120 
SNSNRRNIYK NDYSTNLRDF SFANLKQNSE RNKDGHEIQI NTSMPANTNG QQKRFSPSLP 

       130        140        150        160        170        180 
SAVSFTVPEV ERLPYHRYSI SNKPGKQQQQ QEQLQQNQQQ EEQQKAQLQE QNQRAKQQEE 

       190        200        210        220        230        240 
VKQIQEQVQK KQTERQQLID EKERIANAIF KENTTNDGTD IRKHSVSSGT SNSEDEVDSP 

       250        260        270        280        290        300 
SMEKNSIVHM PGDFIYFNPK SNASKPITAK AAPLSANNST HKNKEVITAP TGPRVPFTEF 

       310        320        330        340        350        360 
FQKEDDKKFH ILIGATGSVA TIKVPLIIDK LFKIYGPEKI SIQLIVTKPA EHFLKGLKMS 

       370        380        390        400        410        420 
THVKIWREED AWVFDAVNKN DTSLSLNLIL HHELRKWADI FLIAPLSANT LAKLANGICN 

       430        440        450        460        470        480 
NLLTSVMRDW SPLTPVLIAP AMNTFMYINP MTKKHLTSLV QDYPFIQVLK PVEKVLICGD 

       490        500        510        520        530        540 
IGMGGMREWT DIVEIVRRRI NEIRKARDEE TGDKEQEQEE QEGADNEDDD DEDDEEDEED 

       550        560        570 
EEEEEALNET ASDESNDEED EEDEEDVKTE V

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, MASS SPECTROMETRY. Strain: YAL6B.
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-116; SER-121 AND SER-124, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, MASS SPECTROMETRY.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; THR-230; SER-231 AND SER-239, MASS SPECTROMETRY.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-116; SER-118; SER-233 AND SER-264, MASS SPECTROMETRY.
[10]	"Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces cerevisiae: identification of a conditional mutation in the pantothenate kinase gene CAB1." Olzhausen J., Schuebbe S., Schueller H.-J. Curr. Genet. 55:163-173(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis." Ruiz A., Gonzalez A., Munoz I., Serrano R., Abrie J.A., Strauss E., Arino J. Nat. Chem. Biol. 5:920-928(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-478, INTERACTION WITH HAL3 AND VHS3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z28088 Genomic DNA. Translation: CAA81926.1. BK006944 Genomic DNA. Translation: DAA09070.1.
PIR	S37913.
RefSeq	NP_012835.1. NM_001179654.1.
3D structure databases
ProteinModelPortal	P36076.
SMR	P36076. Positions 307-497.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4475N.
IntAct	P36076. 67 interactions.
MINT	MINT-541287.
STRING	4932.YKL088W.
Proteomic databases
PaxDb	P36076.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL088W; YKL088W; YKL088W.
GeneID	853774.
KEGG	sce:YKL088W.
Organism-specific databases
CYGD	YKL088w.
SGD	S000001571. CAB3.
Phylogenomic databases
eggNOG	COG0452.
GeneTree	ENSGT00440000038107.
KO	K01598.
OMA	ISIQLIV.
OrthoDB	EOG4J9R82.
Gene expression databases
Genevestigator	P36076.
GermOnline	YKL088W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.50.1950. 1 hit.
InterPro	IPR003382. Flavoprotein. [Graphical view]
Pfam	PF02441. Flavoprotein. 1 hit. [Graphical view]
SUPFAM	SSF52507. Flavoprotein. 1 hit.
ProtoNet	Search...
Other
NextBio	974879.

Entry information

Entry name

CAB3_YEAST

Accession

Primary (citable) accession number: P36076
Secondary accession number(s): D6VXK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents