Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pantothenate synthetase

Gene

panC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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

Pathway: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Pantothenate synthetase (panC)
This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371Proton donorUniRule annotation
Binding sitei61 – 611Beta-alanineUniRule annotation
Binding sitei61 – 611PantoateUniRule annotation
Binding sitei153 – 1531PantoateUniRule annotation
Binding sitei176 – 1761ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378ATPUniRule annotation
Nucleotide bindingi147 – 1504ATPUniRule annotation
Nucleotide bindingi184 – 1874ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU22420-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:BSU22420
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU22420. [Micado]

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Pantothenate synthetasePRO_0000128204Add
BLAST

Proteomic databases

PRIDEiP52998.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100012326.

Structurei

3D structure databases

ProteinModelPortaliP52998.
SMRiP52998. Positions 1-279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000175517.
InParanoidiP52998.
KOiK01918.
OMAiEIDYVEV.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP52998.

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]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

P52998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQITDISQL KEAIKQYHSE GKSIGFVPTM GFLHEGHLTL ADKARQENDA
60 70 80 90 100
VIMSIFVNPA QFGPNEDFEA YPRDIERDAA LAENAGVDIL FTPDAHDMYP
110 120 130 140 150
GEKNVTIHVE RRTDVLCGRS REGHFDGVAI VLTKLFNLVK PTRAYFGLKD
160 170 180 190 200
AQQVAVVDGL ISDFFMDIEL VPVDTVREED GLAKSSRNVY LTAEERKEAP
210 220 230 240 250
KLYRALQTSA ELVQAGERDP EAVIKAAKDI IETTSGTIDY VELYSYPELE
260 270 280
PVNEIAGKMI LAVAVAFSKA RLIDNIIIDI REMERI
Length:286
Mass (Da):31,958
Last modified:October 1, 1996 - v1
Checksum:i998D56197E36A3C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47709 Genomic DNA. Translation: AAB38449.1.
AL009126 Genomic DNA. Translation: CAB14158.1.
PIRiH69671.
RefSeqiNP_390123.1. NC_000964.3.
WP_003230656.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14158; CAB14158; BSU22420.
GeneIDi939030.
KEGGibsu:BSU22420.
PATRICi18976293. VBIBacSub10457_2337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47709 Genomic DNA. Translation: AAB38449.1.
AL009126 Genomic DNA. Translation: CAB14158.1.
PIRiH69671.
RefSeqiNP_390123.1. NC_000964.3.
WP_003230656.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP52998.
SMRiP52998. Positions 1-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100012326.

Proteomic databases

PRIDEiP52998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14158; CAB14158; BSU22420.
GeneIDi939030.
KEGGibsu:BSU22420.
PATRICi18976293. VBIBacSub10457_2337.

Organism-specific databases

GenoListiBSU22420. [Micado]

Phylogenomic databases

HOGENOMiHOG000175517.
InParanoidiP52998.
KOiK01918.
OMAiEIDYVEV.
OrthoDBiEOG6Z6FZ4.
PhylomeDBiP52998.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.
BioCyciBSUB:BSU22420-MONOMER.

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]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome."
    Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P.
    Microbiology 142:2005-2016(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiPANC_BACSU
AccessioniPrimary (citable) accession number: P52998
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 101 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.