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Q47KV5

- PANC_THEFY

UniProt

Q47KV5 - PANC_THEFY

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Protein

Pantothenate synthetase

Gene

panC

Organism
Thermobifida fusca (strain YX)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441Proton donorUniRule annotation
Binding sitei68 – 681Beta-alanineUniRule annotation
Binding sitei68 – 681PantoateUniRule annotation
Binding sitei166 – 1661PantoateUniRule annotation
Binding sitei189 – 1891ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 448ATPUniRule annotation
Nucleotide bindingi160 – 1634ATPUniRule annotation
Nucleotide bindingi197 – 2004ATPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. pantothenate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTFUS269800:GI42-2926-MONOMER.
UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate synthetaseUniRule annotation (EC:6.3.2.1UniRule annotation)
Short name:
PSUniRule annotation
Alternative name(s):
Pantoate--beta-alanine ligaseUniRule annotation
Pantoate-activating enzymeUniRule annotation
Gene namesi
Name:panCUniRule annotation
Ordered Locus Names:Tfu_2884
OrganismiThermobifida fusca (strain YX)
Taxonomic identifieri269800 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida
ProteomesiUP000000434: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Pantothenate synthetasePRO_0000305567Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi269800.Tfu_2884.

Structurei

3D structure databases

ProteinModelPortaliQ47KV5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
KOiK01918.
OMAiPTHFAGM.
OrthoDBiEOG6Z6FZ4.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q47KV5 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTQSTASAHK TPVVTRTAEE IQALRPQLGR LALVPTMGAL HTGHRSLIAQ
60 70 80 90 100
AREHAESVAV SIFVNPLQFG PNEDYDRYPR TFDHDLRVCA EEGVDVVFAP
110 120 130 140 150
TVDVMYPDAD GDSLGQIVTV DPGSMGRVLE GEFRPGFFHG VLTVVNKLFN
160 170 180 190 200
LIRPDVAVFG QKDAQQLAVV RRMVRDLCLP VTIVAAPTVR DPDGLATSSR
210 220 230 240 250
NVYLSAEERA SALALSKALF AGADAASSGP AAVLAAARAI LSEAARATPP
260 270 280 290
VSVDYLALVD PTTFTEVGDD YRGDAVLAVA AWVGETRLID NVPLTL
Length:296
Mass (Da):31,543
Last modified:September 13, 2005 - v1
Checksum:i1E1BB5AC186F9E6A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000088 Genomic DNA. Translation: AAZ56917.1.
RefSeqiYP_290940.1. NC_007333.1.

Genome annotation databases

EnsemblBacteriaiAAZ56917; AAZ56917; Tfu_2884.
GeneIDi3581789.
KEGGitfu:Tfu_2884.
PATRICi23906532. VBITheFus33945_3066.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000088 Genomic DNA. Translation: AAZ56917.1 .
RefSeqi YP_290940.1. NC_007333.1.

3D structure databases

ProteinModelPortali Q47KV5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269800.Tfu_2884.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ56917 ; AAZ56917 ; Tfu_2884 .
GeneIDi 3581789.
KEGGi tfu:Tfu_2884.
PATRICi 23906532. VBITheFus33945_3066.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175516.
KOi K01918.
OMAi PTHFAGM.
OrthoDBi EOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci TFUS269800:GI42-2926-MONOMER.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi IPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF02569. Pantoate_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: YX.

Entry informationi

Entry nameiPANC_THEFY
AccessioniPrimary (citable) accession number: Q47KV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 13, 2005
Last modified: October 29, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism.UniRule annotation

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

External Data

Dasty 3