Reviewed, UniProtKB/Swiss-Prot P31663 (PANC_ECOLI)

Names and origin

Protein names

Recommended name:
    Pantothenate synthetase
      Short name=PS
    EC=6.3.2.1
Alternative name(s):
    Pantoate--beta-alanine ligase
    Pantoate-activating enzyme

Gene names

Name:	panC
Ordered Locus Names:	b0133, JW0129

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Ref.4
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158
Enzyme regulation	Activation requires a combination of a divalent cation, magnesium or manganese, and a monovalent cation, potassium or ammonium. Above the optimum concentration for activation, magnesium and manganese are rather inhibitory. Also activated by 2-mercaptoethanol, dithiothreitol, cysteine and glutathione. Inhibited by divalent cations (mercury, cobalt, zinc, copper, silver), chelating agents (EDTA, EGTA and o-phenanthroline), and analogs of beta-alanine (taurine, gamma-aminobutyrate, gamma-amino-beta-hydroxybutyrate). Ref.4
Pathway	Cofactor biosynthesis; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: step 1/1. HAMAP MF_00158
Subunit structure	Homodimer. Ref.5
Subcellular location	Cytoplasm Potential.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism. HAMAP MF_00158
Sequence similarities	Belongs to the pantothenate synthetase family.
biophysicochemical properties	Kinetic parameters: KM=63 µM for pantoate HAMAP MF_00158 KM=100 µM for ATP KM=150 µM for beta-alanine KM=2000 µM for magnesium KM=5500 µM for manganese pH dependence: Optimum pH is 10. Stable from pH 5.0 to 11.0. Temperature dependence: Optimum temperature is 30 degrees Celsius. Stable up to 37 degrees Celsius and loses activity almost completely when incubated at 60 degrees Celsius for 10 minutes.
Mass spectrometry	Molecular mass is 31601.2±3.4 Da from positions 1 - 283. Determined by ESI. Ref.5

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantoate-beta-alanine ligase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
yfcD	P65556	2	EBI-545354,EBI-545346

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 283

283

Pantothenate synthetase HAMAP MF_00158

PRO_0000128229

Regions

Nucleotide binding

30 – 37

8

ATP By similarity

Nucleotide binding

149 – 152

4

ATP By similarity

Nucleotide binding

186 – 189

4

ATP By similarity

Sites

Active site

37

1

Proton donor By similarity

Binding site

61

1

Beta-alanine By similarity

Binding site

61

1

Pantoate By similarity

Binding site

155

1

Pantoate By similarity

Binding site

178

1

ATP; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

1

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283

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Helix

7 – 19

13

Beta strand

24 – 29

6

Helix

35 – 47

13

Beta strand

49 – 55

7

Helix

59 – 61

3

Helix

65 – 70

6

Helix

75 – 84

10

Beta strand

88 – 91

4

Helix

95 – 98

4

Beta strand

108 – 110

3

Helix

114 – 116

3

Helix

119 – 122

4

Helix

126 – 141

16

Beta strand

144 – 149

6

Helix

153 – 166

14

Beta strand

171 – 175

5

Helix

188 – 192

5

Helix

195 – 200

6

Helix

203 – 216

14

Helix

222 – 236

15

Beta strand

239 – 247

9

Turn

248 – 250

3

Beta strand

260 – 269

10

Beta strand

272 – 281

10

Sequences

	Sequence		Length	Mass (Da)
	P31663-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 4246647C6FDAFB20	FASTA	283	31,598
	10 20 30 40 50 60 MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV VVVSIFVNPM 70 80 90 100 110 120 QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP NGTETHTYVD VPGLSTMLEG 130 140 150 160 170 180 ASRPGHFRGV STIVSKLFNL VQPDIACFGE KDFQQLALIR KMVADMGFDI EIVGVPIMRA 190 200 210 220 230 240 KDGLALSSRN GYLTAEQRKI APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA 250 260 270 280 DDIQIRDADT LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and sequence of the Escherichia coli panBCD gene cluster." Merkel W.K., Nichols B.P. FEMS Microbiol. Lett. 143:247-252(1996) [PubMed: 8837478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Enzymological properties of pantothenate synthetase from Escherichia coli B." Miyatake K., Nakano Y., Kitaoka S. J. Nutr. Sci. Vitaminol. 24:243-253(1978) [PubMed: 357689] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ENZYME REGULATION. Strain: B.
[5]	"The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily." von Delft F., Lewendon A., Dhanaraj V., Blundell T.L., Abell C., Smith A.G. Structure 9:439-450(2001) [PubMed: 11377204] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MASS SPECTROMETRY, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L17086 Genomic DNA. Translation: AAA24272.1.
U00096 Genomic DNA. Translation: AAC73244.1.
AP009048 Genomic DNA. Translation: BAE76042.1.

PIR

E64736.

RefSeq

AP_000794.1.
NP_414675.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IHO	X-ray	1.70	A/B	1-283	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10437N.

IntAct

P31663. 11 interactions.

2-D gel databases

SWISS-2DPAGE

P31663.

Genome annotation databases

GeneID

944958.

GenomeReviews

Gene locus JW0129 in contig AP009048_GR.
Gene locus b0133 in contig U00096_GR.

KEGG

ecj:JW0129.
eco:b0133.

Organism-specific databases

EchoBASE

EB1696.

EcoGene

EG11746. panC.

CMR

Search...

Phylogenomic databases

HOGENOM

P31663.

OMA

P31663. SRNVYLN.

Enzyme and pathway databases

BioCyc

EcoCyc:PANTOATE-BETA-ALANINE-LIG-MON.
MetaCyc:PANTOATE-BETA-ALANINE-LIG-MON.

Family and domain databases

HAMAP

MF_00158.
[Tree]

InterPro

IPR004821. Cyt_trans_rel.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

PANTHER

PTHR21299:SF1. Pantoate_ligase. 1 hit.

Pfam

PF02569. Pantoate_ligase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PANC_ECOLI

Accession

Primary (citable) accession number: P31663
Secondary accession number(s): Q2MCG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)