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Protein

Pantoate--beta-alanine ligase

Gene

PAN6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for pantothenic acid biosynthesis.1 Publication

Catalytic activityi

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. pantoate-beta-alanine ligase activity Source: SGD

GO - Biological processi

  1. pantothenate biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YIL145C-MONOMER.
YEAST:YIL145C-MONOMER.
UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantoate--beta-alanine ligase (EC:6.3.2.1)
Alternative name(s):
Pantoate-activating enzyme
Pantothenate synthetase
Gene namesi
Name:PAN6
Ordered Locus Names:YIL145C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL145c.
SGDiS000001407. PAN6.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Pantoate--beta-alanine ligasePRO_0000128298Add
BLAST

Proteomic databases

MaxQBiP40459.
PaxDbiP40459.
PeptideAtlasiP40459.

Expressioni

Gene expression databases

GenevestigatoriP40459.

Interactioni

Protein-protein interaction databases

BioGridi34847. 19 interactions.
DIPiDIP-4613N.
IntActiP40459. 2 interactions.
MINTiMINT-560279.
STRINGi4932.YIL145C.

Structurei

3D structure databases

ProteinModelPortaliP40459.
SMRiP40459. Positions 1-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
InParanoidiP40459.
KOiK01918.
OMAiRTWDSDV.
OrthoDBiEOG7V1G1D.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

P40459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIFHTVEEV VQWRTQELRE TRFRETIGFV PTMGCLHSGH ASLISQSVKE
60 70 80 90 100
NTYTVVSIFV NPSQFAPTED LDNYPRTLPD DIKLLESLKV DVLFAPNAHV
110 120 130 140 150
MYPQGIPLDI EEQKGPFVSV LGLSEKLEGK TRPNFFRGVA TVVTKLFNIV
160 170 180 190 200
MADVAYFGQK DIQQFIVLQC MVDELFVNTR LQMMPIVRNN NGLALSSRNK
210 220 230 240 250
YLCPESLKIS ENLYRGLKAA ENAIRRLAPG GRLSRSEIID TVTQIWAPYV
260 270 280 290 300
DSHDFKIDYV SLADFKTLDE LSDVENTSEQ QPIVISCAVY VTDREKPDTV

VRLIDNIVI
Length:309
Mass (Da):35,032
Last modified:December 20, 2005 - v2
Checksum:i9787B366795B5D81
GO

Sequence cautioni

The sequence CAA86133.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA. Translation: CAA86133.1. Different initiation.
BK006942 Genomic DNA. Translation: DAA08408.1.
PIRiS48389.
RefSeqiNP_012121.2. NM_001179493.1.

Genome annotation databases

EnsemblFungiiYIL145C; YIL145C; YIL145C.
GeneIDi854661.
KEGGisce:YIL145C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA. Translation: CAA86133.1. Different initiation.
BK006942 Genomic DNA. Translation: DAA08408.1.
PIRiS48389.
RefSeqiNP_012121.2. NM_001179493.1.

3D structure databases

ProteinModelPortaliP40459.
SMRiP40459. Positions 1-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34847. 19 interactions.
DIPiDIP-4613N.
IntActiP40459. 2 interactions.
MINTiMINT-560279.
STRINGi4932.YIL145C.

Proteomic databases

MaxQBiP40459.
PaxDbiP40459.
PeptideAtlasiP40459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL145C; YIL145C; YIL145C.
GeneIDi854661.
KEGGisce:YIL145C.

Organism-specific databases

CYGDiYIL145c.
SGDiS000001407. PAN6.

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
InParanoidiP40459.
KOiK01918.
OMAiRTWDSDV.
OrthoDBiEOG7V1G1D.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.
BioCyciMetaCyc:YIL145C-MONOMER.
YEAST:YIL145C-MONOMER.

Miscellaneous databases

NextBioi977232.

Gene expression databases

GenevestigatoriP40459.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Saccharomyces cerevisiae is capable of de novo pantothenic acid biosynthesis involving a novel pathway of beta-alanine production from spermine."
    White W.H., Gunyuzlu P.L., Toyn J.H.
    J. Biol. Chem. 276:10794-10800(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPANC_YEAST
AccessioniPrimary (citable) accession number: P40459
Secondary accession number(s): D6VVE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 20, 2005
Last modified: January 7, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.