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Protein

4-phosphopantoate--beta-alanine ligase

Gene

TK1686

Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. Cannot use (R)-pantoate as substrate and thus does not display pantothenate synthetase (PS) activity.1 Publication

Catalytic activityi

ATP + (R)-4-phosphopantoate + beta-alanine = AMP + diphosphate + (R)-4'-phosphopantothenate.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15971.
TKOD69014:GH72-1718-MONOMER.
BRENDAi6.3.2.26. 5246.
6.3.2.36. 5246.

Names & Taxonomyi

Protein namesi
Recommended name:
4-phosphopantoate--beta-alanine ligase (EC:6.3.2.36)
Alternative name(s):
Phosphopantothenate synthetase
Short name:
PPS
Gene namesi
Ordered Locus Names:TK1686
OrganismiThermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Taxonomic identifieri69014 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
Proteomesi
  • UP000000536 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Only viable in the presence of CoA or 4'-phosphopantothenate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2612614-phosphopantoate--beta-alanine ligasePRO_0000409260Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi69014.TK1686.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2515Combined sources
Helixi31 – 4717Combined sources
Helixi53 – 6816Combined sources
Beta strandi73 – 764Combined sources
Helixi78 – 836Combined sources
Helixi85 – 9511Combined sources
Beta strandi98 – 1014Combined sources
Helixi108 – 11912Combined sources
Beta strandi137 – 1393Combined sources
Helixi141 – 1433Combined sources
Turni148 – 1503Combined sources
Helixi151 – 1533Combined sources
Beta strandi155 – 1584Combined sources
Helixi164 – 1729Combined sources
Beta strandi176 – 1805Combined sources
Helixi187 – 1915Combined sources
Beta strandi192 – 1965Combined sources
Helixi200 – 21314Combined sources
Turni214 – 2163Combined sources
Helixi219 – 2279Combined sources
Helixi231 – 25222Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WDKX-ray2.30A/B/C/D1-261[»]
3WDLX-ray2.40A/B/C/D1-261[»]
3WDMX-ray2.00A/B/C/D1-261[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG04262. Archaea.
COG1701. LUCA.
HOGENOMiHOG000230027.
InParanoidiQ5JIZ8.
KOiK09722.
OMAiPKSHPRY.

Family and domain databases

InterProiIPR002855. PPS.
[Graphical view]
PfamiPF02006. DUF137. 1 hit.
[Graphical view]
PIRSFiPIRSF004853. UCP004853. 1 hit.
ProDomiPD016827. DUF137. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q5JIZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNIPKSHPR YWSLYYREKI IEGMEKGMTA KAGLIAHGRG EAFDYLIGER
60 70 80 90 100
TIEPAERAMR AAVAKFLLAE HPVISVNGNV AALVPKETIE LAKALNAKLE
110 120 130 140 150
INLFYRTEER VRTIAEELRK YDPEIEILGI NPTKRIPGLE HERGKVDENG
160 170 180 190 200
IWKADVVLVP LEDGDRTEAL VRMGKFVVTV DLNPLSRSAR MADITIVDNI
210 220 230 240 250
VRAYPRMVEL AREMKDYSRE ELLKIVGEYD NGKTLSDVLL HIRDRLTRLA
260
EEGIWRRKEL E
Length:261
Mass (Da):29,845
Last modified:February 15, 2005 - v1
Checksum:iD36C99384454D82E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006878 Genomic DNA. Translation: BAD85875.1.
RefSeqiWP_011250637.1. NC_006624.1.

Genome annotation databases

EnsemblBacteriaiBAD85875; BAD85875; TK1686.
GeneIDi3235144.
KEGGitko:TK1686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006878 Genomic DNA. Translation: BAD85875.1.
RefSeqiWP_011250637.1. NC_006624.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WDKX-ray2.30A/B/C/D1-261[»]
3WDLX-ray2.40A/B/C/D1-261[»]
3WDMX-ray2.00A/B/C/D1-261[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi69014.TK1686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD85875; BAD85875; TK1686.
GeneIDi3235144.
KEGGitko:TK1686.

Phylogenomic databases

eggNOGiarCOG04262. Archaea.
COG1701. LUCA.
HOGENOMiHOG000230027.
InParanoidiQ5JIZ8.
KOiK09722.
OMAiPKSHPRY.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15971.
TKOD69014:GH72-1718-MONOMER.
BRENDAi6.3.2.26. 5246.
6.3.2.36. 5246.

Family and domain databases

InterProiIPR002855. PPS.
[Graphical view]
PfamiPF02006. DUF137. 1 hit.
[Graphical view]
PIRSFiPIRSF004853. UCP004853. 1 hit.
ProDomiPD016827. DUF137. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
    Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
    Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-918 / JCM 12380 / KOD1.
  2. "Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the Archaea."
    Yokooji Y., Tomita H., Atomi H., Imanaka T.
    J. Biol. Chem. 284:28137-28145(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, ROLE IN COA BIOSYNTHESIS, SUBUNIT, DISRUPTION PHENOTYPE.
    Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Entry informationi

Entry nameiPPS_THEKO
AccessioniPrimary (citable) accession number: Q5JIZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: February 15, 2005
Last modified: November 11, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.