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O34098 (SPOT_SPICI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase

EC=3.1.7.2
Alternative name(s):
Penta-phosphate guanosine-3'-pyrophosphohydrolase
Short name=(ppGpp)ase
Gene names
Name:spoT
OrganismSpiroplasma citri
Taxonomic identifier2133 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesEntomoplasmatalesSpiroplasmataceaeSpiroplasma

Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the degradation of ppGpp into GDP. It may also be capable of catalyzing the synthesis of ppGpp By similarity.

Catalytic activity

Guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.

Cofactor

Manganese By similarity.

Pathway

Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.

Sequence similarities

Belongs to the RelA/SpoT family.

Contains 1 ACT domain.

Contains 1 HD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 749749Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase
PRO_0000166575

Regions

Domain49 – 148100HD
Domain674 – 74976ACT

Sequences

Sequence LengthMass (Da)Tools
O34098 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: D32992E612317042

FASTA74986,282
        10         20         30         40         50         60 
MDRDIKYEEV LAQIKLYIKD EATLKEIQKA YEYAEEKHHG QVRNSGARYI IHPLWTTFFL 

        70         80         90        100        110        120 
AQWRMGPKTL IAGLLHDVLE DTPATFEELQ ELFGIEIANL VEGVTKVSYF AKENRTQIKA 

       130        140        150        160        170        180 
QYLRKLYLSM AKDIRVIIVK LADRLHNLKT IGYLKPERQQ IIARESLEIY SAIAHRLGMK 

       190        200        210        220        230        240 
AVKQEIEDIS FKIINPVQYN KIVSLLESSN KERENTINQK IEELKKILIT EKKMSVKVYG 

       250        260        270        280        290        300 
RSKSIYSIYR KMNQFGKNFD DIHDILAVRI ITNSVDDCYK VLGFVHQHYT PLNNRFKDYI 

       310        320        330        340        350        360 
ATPKHNLYQS LHTTIVADDG LIFEVQIRTE EMDELAEQGV AAHWRYKEGE NYDIAKKQKD 

       370        380        390        400        410        420 
IDERLDIFKR ILDLENISVQ ERDEIQQEVY KPDHLMEQII QNDIFSSLIY VLTPNGKVVT 

       430        440        450        460        470        480 
LPFGSTVLDF AYKIHSEIGE KTIGAKINGL FSPISTVLKS GDVVDIKTAA TQKPNHSWLV 

       490        500        510        520        530        540 
VSKTSSALEK IKKYLKKELV EVTSDAKSVN LEKIKQTKSQ IEEYIAKKDL KWKLVNSETQ 

       550        560        570        580        590        600 
LERLHAINFN NIEDFLLDVA NDEYTLEEAI NLVYLDHETS QNEKILKKLQ DKQYKKAQLK 

       610        620        630        640        650        660 
DDIIVQGISN IKVVISQCCL PIPYEDITGY VSKAEGIKVH LKTCRNIQSG DKQDRQVEVS 

       670        680        690        700        710        720 
WNEAVCKNKQ YDCAIRIEAI DRPALLVDVT KVLSHLNASV QMMSANVSGD LMNLTIKTII 

       730        740 
KVSNADRLQQ IRSSLLTIPD IKVVERVMM 

« Hide

References

[1]"Isolation, characterization, and complementation of a motility mutant of Spiroplasma citri."
Jacob C., Nouzieres F., Duret S., Bove J.M., Renaudin J.
J. Bacteriol. 179:4802-4810(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GII-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89875 Genomic DNA. Translation: AAC45548.1.

3D structure databases

ProteinModelPortalO34098.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00908; UER00886.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamPF01842. ACT. 1 hit.
PF01966. HD. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
SMARTSM00471. HDc. 1 hit.
SM00954. RelA_SpoT. 1 hit.
[Graphical view]
SUPFAMSSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00691. spoT_relA. 1 hit.
PROSITEPS51671. ACT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPOT_SPICI
AccessionPrimary (citable) accession number: O34098
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways