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Protein

Manganese-dependent inorganic pyrophosphatase

Gene

ppaC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mn2+Note: Binds 2 manganese ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9Manganese 11
Metal bindingi13Manganese 11
Metal bindingi15Manganese 21
Metal bindingi75Manganese 11
Metal bindingi75Manganese 21
Metal bindingi97Manganese 21
Metal bindingi149Manganese 21

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU40550-MONOMER.
BRENDAi3.6.1.1. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese-dependent inorganic pyrophosphatase (EC:3.6.1.1)
Alternative name(s):
Pyrophosphate phospho-hydrolase
Short name:
PPase
Gene namesi
Name:ppaC
Ordered Locus Names:BSU40550
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001585681 – 309Manganese-dependent inorganic pyrophosphataseAdd BLAST309

Proteomic databases

PaxDbiP37487.
PRIDEiP37487.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP37487. 1 interactor.
MINTiMINT-8365645.
STRINGi224308.Bsubs1_010100021886.

Structurei

Secondary structure

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Helixi14 – 29Combined sources16
Beta strandi34 – 40Combined sources7
Helixi44 – 52Combined sources9
Turni65 – 67Combined sources3
Beta strandi69 – 75Combined sources7
Helixi79 – 81Combined sources3
Helixi86 – 88Combined sources3
Beta strandi89 – 96Combined sources8
Beta strandi110 – 113Combined sources4
Beta strandi115 – 117Combined sources3
Helixi119 – 129Combined sources11
Helixi136 – 150Combined sources15
Turni151 – 154Combined sources4
Helixi160 – 173Combined sources14
Helixi177 – 187Combined sources11
Helixi196 – 199Combined sources4
Turni200 – 203Combined sources4
Beta strandi204 – 209Combined sources6
Beta strandi212 – 222Combined sources11
Helixi224 – 228Combined sources5
Helixi231 – 244Combined sources14
Beta strandi248 – 256Combined sources9
Turni257 – 260Combined sources4
Beta strandi261 – 268Combined sources8
Turni269 – 271Combined sources3
Helixi272 – 278Combined sources7
Beta strandi286 – 290Combined sources5
Helixi295 – 298Combined sources4
Helixi300 – 307Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K23X-ray3.00A/B/C/D1-309[»]
1WPMX-ray2.05A/B1-309[»]
1WPNX-ray1.30A/B1-188[»]
2HAWX-ray1.75A/B1-309[»]
2IW4X-ray2.15A/B1-309[»]
ProteinModelPortaliP37487.
SMRiP37487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37487.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPase class C family.Curated

Phylogenomic databases

eggNOGiENOG4105E2M. Bacteria.
COG1227. LUCA.
HOGENOMiHOG000223999.
InParanoidiP37487.
KOiK15986.
OMAiMLCAILS.
PhylomeDBiP37487.

Family and domain databases

HAMAPiMF_00207. PPase_C. 1 hit.
InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
IPR022934. Mn-dep_inorganic_PyrPase.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKILIFGHQ NPDTDTICSA IAYADLKNKL GFNAEPVRLG QVNGETQYAL
60 70 80 90 100
DYFKQESPRL VETAANEVNG VILVDHNERQ QSIKDIEEVQ VLEVIDHHRI
110 120 130 140 150
ANFETAEPLY YRAEPVGCTA TILNKMYKEN NVKIEKEIAG LMLSAIISDS
160 170 180 190 200
LLFKSPTCTD QDVAAAKELA EIAGVDAEEY GLNMLKAGAD LSKKTVEELI
210 220 230 240 250
SLDAKEFTLG SKKVEIAQVN TVDIEDVKKR QAELEAVISK VVAEKNLDLF
260 270 280 290 300
LLVITDILEN DSLALAIGNE AAKVEKAFNV TLENNTALLK GVVSRKKQVV

PVLTDAMAE
Length:309
Mass (Da):33,989
Last modified:October 1, 1994 - v1
Checksum:i5C27CCC20D71B941
GO

Mass spectrometryi

Molecular mass is 34019 Da from positions 1 - 309. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05186.1.
AL009126 Genomic DNA. Translation: CAB16092.1.
PIRiS65980.
RefSeqiNP_391935.1. NC_000964.3.
WP_003226902.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB16092; CAB16092; BSU40550.
GeneIDi937817.
KEGGibsu:BSU40550.
PATRICi18980198. VBIBacSub10457_4257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05186.1.
AL009126 Genomic DNA. Translation: CAB16092.1.
PIRiS65980.
RefSeqiNP_391935.1. NC_000964.3.
WP_003226902.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K23X-ray3.00A/B/C/D1-309[»]
1WPMX-ray2.05A/B1-309[»]
1WPNX-ray1.30A/B1-188[»]
2HAWX-ray1.75A/B1-309[»]
2IW4X-ray2.15A/B1-309[»]
ProteinModelPortaliP37487.
SMRiP37487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37487. 1 interactor.
MINTiMINT-8365645.
STRINGi224308.Bsubs1_010100021886.

Proteomic databases

PaxDbiP37487.
PRIDEiP37487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16092; CAB16092; BSU40550.
GeneIDi937817.
KEGGibsu:BSU40550.
PATRICi18980198. VBIBacSub10457_4257.

Phylogenomic databases

eggNOGiENOG4105E2M. Bacteria.
COG1227. LUCA.
HOGENOMiHOG000223999.
InParanoidiP37487.
KOiK15986.
OMAiMLCAILS.
PhylomeDBiP37487.

Enzyme and pathway databases

BioCyciBSUB:BSU40550-MONOMER.
BRENDAi3.6.1.1. 658.

Miscellaneous databases

EvolutionaryTraceiP37487.
PROiP37487.

Family and domain databases

HAMAPiMF_00207. PPase_C. 1 hit.
InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
IPR022934. Mn-dep_inorganic_PyrPase.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPAC_BACSU
AccessioniPrimary (citable) accession number: P37487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.