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Reviewed, UniProtKB/Swiss-Prot P37564 (COAX_BACSU)

Last modified November 24, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Type III pantothenate kinase
    EC=2.7.1.33
Alternative name(s):
    Pantothenic acid kinase
    PanK-III
Gene names
Name: coaX
Synonyms: coaA, yacB
Ordered Locus Names: BSU00700
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can not utilize a phosphoryl donor other than ATP. Ref.1 Ref.5

Catalytic activity

ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. HAMAP MF_01274

Cofactor

Monovalent cations. Ammonium or potassium. Ref.5

Enzyme regulation

Not regulated by feedback inhibition by CoA and its thioesters as described for many other pantothenate kinases. Not inhibited by N-pentylpantothenamide (N5-Pan), and this compound can not act as a substrate either. Ref.1

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. HAMAP MF_01274

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the type III pantothenate kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=168 µM for pantothenate Ref.1

KM=3.0 mM for ATP

Sequence caution

The sequence BAA05305.1 differs from that shown. Reason: Frameshift at position 214.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Type III pantothenate kinase HAMAP MF_01274
PRO_0000049448

Regions

Nucleotide binding6 – 138ATP By similarity
Region107 – 1104Substrate binding By similarity

Sites

Active site1091Proton acceptor Potential
Metal binding1291Monovalent cation Potential
Binding site1001Substrate By similarity
Binding site1321ATP Potential
Binding site1841Substrate By similarity

Experimental info

Sequence conflict214 – 2152EP → KQ in AAW83041. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37564-1 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: EB2BB7FECE46DEA2

FASTA25828,576
        10         20         30         40         50         60 
MLLVIDVGNT NTVLGVYHDG KLEYHWRIET SRHKTEDEFG MILRSLFDHS GLMFEQIDGI 

        70         80         90        100        110        120 
IISSVVPPIM FALERMCTKY FHIEPQIVGP GMKTGLNIKY DNPKEVGADR IVNAVAAIHL 

       130        140        150        160        170        180 
YGNPLIVVDF GTATTYCYID ENKQYMGGAI APGITISTEA LYSRAAKLPR IEITRPDNII 

       190        200        210        220        230        240 
GKNTVSAMQS GILFGYVGQV EGIVKRMKWQ AKQEPKVIAT GGLAPLIANE SDCIDIVDPF 

       250 
LTLKGLELIY ERNRVGSV 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a new pantothenate kinase isoform from Helicobacter pylori."
Brand L.A., Strauss E.
J. Biol. Chem. 280:20185-20188(2005) [PubMed: 15795230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CHARACTERIZATION, ENZYME REGULATION, KINETIC PARAMETERS.
Strain: 168.
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"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. expand/collapse author list , 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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[5]"Prokaryotic type II and type III pantothenate kinases: the same monomer fold creates dimers with distinct catalytic properties."
Hong B.S., Yun M.K., Zhang Y.-M., Chohnan S., Rock C.O., White S.W., Jackowski S., Park H.-W., Leonardi R.
Structure 14:1251-1261(2006) [PubMed: 16905099] [Abstract]
Cited for: FUNCTION, COFACTOR.
Strain: 168.

Cross-references

Sequence databases

AY912104 Genomic DNA. Translation: AAW83041.2.
D26185 Genomic DNA. Translation: BAA05305.1. Frameshift.
AL009126 Genomic DNA. Translation: CAB11846.2.
PIRS66100.
RefSeqNP_387951.2.

3D structure databases

SMRP37564. Positions 1-253.
ModBaseSearch...

Genome annotation databases

GeneID936960.
GenomeReviewsGene locus BSU00700 in contig AL009126_GR.
KEGGbsu:BSU00700.

Organism-specific databases

SubtiListBG10133. yacB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP37564.

Enzyme and pathway databases

BRENDA2.7.1.33. 150.

Family and domain databases

HAMAPMF_01274.
[Tree]
InterProIPR004619. Baf.
[Graphical view]
PfamPF03309. Bvg_acc_factor. 1 hit.
[Graphical view]
TIGRFAMsTIGR00671. baf. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOAX_BACSU
AccessionPrimary (citable) accession number: P37564
Secondary accession number(s): Q5EC36
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: June 16, 2009
Last modified: November 24, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents