Q2FV22 (PANC_STAA8) Reviewed, UniProtKB/Swiss-Prot

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:	SAOUHSC_02918

Organism

Staphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
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 By similarity. HAMAP-Rule MF_00158
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00158.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP-Rule MF_00158
Sequence similarities	Belongs to the pantothenate synthetase family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantoate-beta-alanine ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 283

283

Pantothenate synthetase HAMAP-Rule MF_00158

PRO_0000305560

Regions

Nucleotide binding

31 – 38

8

ATP By similarity

Nucleotide binding

148 – 151

4

ATP By similarity

Nucleotide binding

185 – 188

4

ATP By similarity

Sites

Active site

38

1

Proton donor By similarity

Binding site

62

1

Beta-alanine By similarity

Binding site

62

1

Pantoate By similarity

Binding site

154

1

Pantoate By similarity

Binding site

177

1

ATP; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

283

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

8 – 20

13

Beta strand

25 – 30

6

Helix

36 – 46

11

Beta strand

49 – 56

8

Helix

60 – 62

3

Turn

69 – 71

3

Helix

76 – 86

11

Beta strand

89 – 92

4

Helix

96 – 99

4

Beta strand

105 – 110

6

Helix

112 – 114

3

Helix

118 – 121

4

Helix

125 – 140

16

Beta strand

143 – 148

6

Helix

149 – 151

3

Helix

152 – 164

13

Beta strand

170 – 174

5

Helix

187 – 191

5

Helix

194 – 199

6

Helix

202 – 215

14

Helix

221 – 235

15

Beta strand

238 – 247

10

Turn

248 – 250

3

Beta strand

261 – 268

8

Beta strand

273 – 280

8

Sequences

	Sequence		Length	Mass (Da)
	Q2FV22 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 553C07138066CC97	FASTA	283	31,534
	10 20 30 40 50 60 MTKLITTVKE MQHIVKAAKR SGTTIGFIPT MGALHDGHLT MVRESVSTND ITIVSVFVNP 70 80 90 100 110 120 LQFGPNEDFD AYPRQIDKDL ELVSEVGADI VFHPAVEDMY PGELGIDVKV GPLADVLEGA 130 140 150 160 170 180 KRPGHFDGVV TVVNKLFNIV MPDYAYFGKK DAQQLAIVEQ MVKDFNHAVE IIGIDIVREA 190 200 210 220 230 240 DGLAKSSRNV YLTEQERQEA VHLSKSLLLA QALYQDGERQ SKVIIDRVTE YLESHISERI 250 260 270 280 EEVAVYSYPQ LVEQHEITGR IFISLAVKFS KARLIDNIII GAE

References

[1]	"The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 8325.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000253 Genomic DNA. Translation: ABD31913.1.

RefSeq

YP_501370.1. NC_007795.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AG5	X-ray	2.50	A/B	1-283	[»]
3AG6	X-ray	1.85	A/B	1-283	[»]

ProteinModelPortal

Q2FV22.

SMR

Q2FV22. Positions 1-283.

ModBase

Search...

Protein-protein interaction databases

STRING

93061.SAOUHSC_02918.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ABD31913; ABD31913; SAOUHSC_02918.

GeneID

3921369.

KEGG

sao:SAOUHSC_02918.

PATRIC

19583063. VBIStaAur99865_2637.

Phylogenomic databases

eggNOG

COG0414.

HOGENOM

HOG000175517.

KO

K01918.

OMA

HTIVSVF.

ProtClustDB

PRK00380.

Enzyme and pathway databases

BioCyc

SAUR93061:GIWJ-2838-MONOMER.

UniPathway

UPA00028; UER00005.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_00158. PanC.

InterPro

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

PANTHER

PTHR21299:SF1. PTHR21299:SF1. 1 hit.

Pfam

PF02569. Pantoate_ligase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00018. panC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PANC_STAA8

Accession

Primary (citable) accession number: Q2FV22

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	March 21, 2006
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program