O67891 (PANC_AQUAE) 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:	aq_2132

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 MF_00158
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158
Subunit structure	Homodimer By similarity. HAMAP MF_00158
Subcellular location	Cytoplasm Potential HAMAP MF_00158.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP 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: UniProtKB-KW
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: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 282

282

Pantothenate synthetase HAMAP MF_00158

PRO_0000128197

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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

282

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

8 – 21

14

Beta strand

25 – 30

6

Helix

36 – 48

13

Beta strand

50 – 56

7

Helix

60 – 62

3

Helix

66 – 71

6

Helix

76 – 86

11

Beta strand

89 – 92

4

Helix

96 – 99

4

Helix

111 – 115

5

Helix

118 – 121

4

Helix

125 – 140

16

Beta strand

143 – 151

9

Helix

152 – 165

14

Beta strand

170 – 174

5

Helix

187 – 191

5

Helix

194 – 200

7

Helix

202 – 216

15

Helix

221 – 234

14

Turn

235 – 238

4

Beta strand

239 – 248

10

Beta strand

259 – 269

11

Beta strand

272 – 281

10

Sequences

	Sequence		Length	Mass (Da)
	O67891 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 7E71B941C158DCEB	FASTA	282	32,433
	10 20 30 40 50 60 MPLLFKKIKD LRNFLKNKRC EGKEIGFVPT MGYLHEGHRQ LIKLARMQND IVVVSIFVNP 70 80 90 100 110 120 TQFGEGEDYD RYPRDLERDL EICEEEGVDV VFAPEVDEIY PKGYRTKVCV GELGKVLEGE 130 140 150 160 170 180 FRPGHFDGVA TIVVKLFNIV QPNRAYFGEK DYQQLKIIEQ VVEDLNIPVE IVPVPIVREE 190 200 210 220 230 240 DGLAYSSRNV YLSPEERESA LSIYKSFLLA EKMIKAGERD AKRIKEAIRA FIERHPHVKG 250 260 270 280 VDYVEITDQN LNPKETVEKG DRILVAVRVG NARLIDNWKV QS

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC07847.1.

PIR

G70482.

RefSeq

NP_214460.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IR7	model	-	A	1-282	[»]

ProteinModelPortal

O67891.

SMR

O67891. Positions 4-279.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1193880.

GenomeReviews

Gene locus aq_2132 in contig AE000657_GR.

KEGG

aae:aq_2132.

NMPDR

fig|224324.1.peg.1475.

PATRIC

20961110. VBIAquAeo85532_1648.

Phylogenomic databases

HOGENOM

HBG428839.

OMA

LNMPIQI.

PhylomeDB

O67891.

ProtClustDB

CLSK2748558.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_2132-MONOMER.

Family and domain databases

HAMAP

MF_00158. PanC.
[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.

KO

K01918.

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_AQUAE

Accession

Primary (citable) accession number: O67891

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program