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Protein

Probable manganese-dependent inorganic pyrophosphatase

Gene

ppaC

Organism
Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
Status
Reviewed-Annotation score: Annotation score: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Manganese 1
Metal bindingi13 – 131Manganese 1
Metal bindingi15 – 151Manganese 2
Metal bindingi77 – 771Manganese 1
Metal bindingi77 – 771Manganese 2
Metal bindingi99 – 991Manganese 2
Metal bindingi151 – 1511Manganese 2

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciSGOR467705:GH3R-1647-MONOMER.
BRENDAi3.6.1.1. 5934.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 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:SGO_1648
OrganismiStreptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
Taxonomic identifieri467705 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000001131 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 311311Probable manganese-dependent inorganic pyrophosphatasePRO_0000158589Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi467705.SGO_1648.

Structurei

Secondary structure

1
311
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi14 – 3118Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 413Combined sources
Helixi45 – 5410Combined sources
Helixi66 – 683Combined sources
Beta strandi71 – 777Combined sources
Helixi81 – 833Combined sources
Helixi88 – 903Combined sources
Beta strandi91 – 988Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi117 – 1193Combined sources
Helixi121 – 13111Combined sources
Helixi138 – 15215Combined sources
Turni153 – 1564Combined sources
Helixi162 – 17514Combined sources
Helixi179 – 18810Combined sources
Helixi198 – 2014Combined sources
Beta strandi204 – 2118Combined sources
Beta strandi214 – 22411Combined sources
Helixi226 – 2305Combined sources
Helixi233 – 24715Combined sources
Beta strandi250 – 2589Combined sources
Turni259 – 2624Combined sources
Beta strandi263 – 2719Combined sources
Helixi273 – 2808Combined sources
Beta strandi288 – 2925Combined sources
Helixi297 – 3004Combined sources
Helixi302 – 3109Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K20X-ray1.50A/B2-311[»]
1WPPX-ray2.05A/B1-311[»]
ProteinModelPortaliP95765.
SMRiP95765. Positions 2-311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP95765.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPase class C family.Curated

Phylogenomic databases

eggNOGiENOG4105E2M. Bacteria.
COG1227. LUCA.
HOGENOMiHOG000223999.
KOiK15986.
OMAiMLCAILS.
OrthoDBiEOG6F81QM.

Family and domain databases

HAMAPiMF_00207. PPase_C.
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.

P95765-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKILVFGHQ NPDSDAIGSS YAFAYLAREA YGLDTEAVAL GEPNEETAFV
60 70 80 90 100
LDYFGVAAPR VITSAKAEGA EQVILTDHNE FQQSVADIAE VEVYGVVDHH
110 120 130 140 150
RVANFETANP LYMRLEPVGS ASSIVYRMFK EHSVAVSKEI AGLMLSGLIS
160 170 180 190 200
DTLLLKSPTT HPTDKAIAPE LAELAGVNLE EYGLAMLKAG TNLASKSAEE
210 220 230 240 250
LIDIDAKTFE LNGNNVRVAQ VNTVDIAEVL ERQAEIEAAI EKAIADNGYS
260 270 280 290 300
DFVLMITDII NSNSEILAIG SNMDKVEAAF NFVLENNHAF LAGAVSRKKQ
310
VVPQLTESFN A
Length:311
Mass (Da):33,541
Last modified:May 1, 1997 - v1
Checksum:i610A704B681E2889
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57759 Genomic DNA. Translation: AAB39104.1.
CP000725 Genomic DNA. Translation: ABV09962.1.
RefSeqiWP_012130706.1. NC_009785.1.

Genome annotation databases

EnsemblBacteriaiABV09962; ABV09962; SGO_1648.
GeneIDi25051201.
KEGGisgo:SGO_1648.
PATRICi19661242. VBIStrGor124371_1622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57759 Genomic DNA. Translation: AAB39104.1.
CP000725 Genomic DNA. Translation: ABV09962.1.
RefSeqiWP_012130706.1. NC_009785.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K20X-ray1.50A/B2-311[»]
1WPPX-ray2.05A/B1-311[»]
ProteinModelPortaliP95765.
SMRiP95765. Positions 2-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi467705.SGO_1648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV09962; ABV09962; SGO_1648.
GeneIDi25051201.
KEGGisgo:SGO_1648.
PATRICi19661242. VBIStrGor124371_1622.

Phylogenomic databases

eggNOGiENOG4105E2M. Bacteria.
COG1227. LUCA.
HOGENOMiHOG000223999.
KOiK15986.
OMAiMLCAILS.
OrthoDBiEOG6F81QM.

Enzyme and pathway databases

BioCyciSGOR467705:GH3R-1647-MONOMER.
BRENDAi3.6.1.1. 5934.

Miscellaneous databases

EvolutionaryTraceiP95765.

Family and domain databases

HAMAPiMF_00207. PPase_C.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Insertional inactivation of an intrageneric coaggregation-relevant adhesin locus from Streptococcus gordonii DL1 (Challis)."
    Whittaker C.J., Clemans D.L., Kolenbrander P.E.
    Infect. Immun. 64:4137-4142(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide."
    Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.
    J. Bacteriol. 189:7799-7807(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288.
  3. "The 'open' and 'closed' structures of the type-C inorganic pyrophosphatases from Bacillus subtilis and Streptococcus gordonii."
    Ahn S., Milner A.J., Fuetterer K., Konopka M., Ilias M., Young T.W., White S.A.
    J. Mol. Biol. 313:797-811(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Entry informationi

Entry nameiPPAC_STRGC
AccessioniPrimary (citable) accession number: P95765
Secondary accession number(s): A8AYR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: July 6, 2016
This is version 109 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.