P37564 (COAX_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type III pantothenate kinase
EC=2.7.1.33

Alternative name(s):
PanK-III
Pantothenic acid kinase

Gene names

Name:	coaX
Synonyms:	coaA, yacB
Ordered Locus Names:	BSU00700

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP MF_01274
Subcellular location	Cytoplasm By similarity HAMAP MF_01274.
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.

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Potassium
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	coenzyme A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pantothenate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 258	258	Type III pantothenate kinase HAMAP MF_01274		PRO_0000049448
Regions
	Nucleotide binding	6 – 13	8	ATP By similarity
	Region	107 – 110	4	Substrate binding By similarity
Sites
	Active site	109	1	Proton acceptor Potential
	Metal binding	129	1	Monovalent cation Potential
	Binding site	100	1	Substrate By similarity
	Binding site	132	1	ATP Potential
	Binding site	184	1	Substrate By similarity
Experimental info
	Sequence conflict	214 – 215	2	EP → KQ in AAW83041. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P37564 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: EB2BB7FECE46DEA2	FASTA	258	28,576
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBL GenBank DDBJ	AY912104 Genomic DNA. Translation: AAW83041.2. D26185 Genomic DNA. Translation: BAA05305.1. Frameshift. AL009126 Genomic DNA. Translation: CAB11846.2.
PIR	S66100.
RefSeq	NP_387951.2. NC_000964.3.
3D structure databases
ProteinModelPortal	P37564.
SMR	P37564. Positions 1-253.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003417; EBBACP00000003417; EBBACG00000003410.
GeneID	936960.
GenomeReviews	Gene locus BSU00700 in contig AL009126_GR.
KEGG	bsu:BSU00700.
PATRIC	18971615. VBIBacSub10457_0071.
Organism-specific databases
GenoList	BSU00700. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002208.
HOGENOM	HBG634537.
PhylomeDB	P37564.
ProtClustDB	PRK13318.
Enzyme and pathway databases
BioCyc	BSUB:BSU00700-MONOMER.
Family and domain databases
HAMAP	MF_01274. Pantothen_kinase_3. [Tree]
InterPro	IPR004619. Type_III_PanK. [Graphical view]
KO	K03525.
Pfam	PF03309. Bvg_acc_factor. 1 hit. [Graphical view]
TIGRFAMs	TIGR00671. Baf. 1 hit.
ProtoNet	Search...

Entry information

Entry name

COAX_BACSU

Accession

Primary (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:	January 25, 2012
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program