Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase

Gene

spoT

Organism
Spiroplasma citri
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathway: ppGpp biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes ppGpp from GDP.
Proteins known to be involved in this subpathway in this organism are:
  1. Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase (spoT)
This subpathway is part of the pathway ppGpp biosynthesis, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ppGpp from GDP, the pathway ppGpp biosynthesis and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese

Enzyme and pathway databases

UniPathwayiUPA00908; UER00886.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:spoT
OrganismiSpiroplasma citri
Taxonomic identifieri2133 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesEntomoplasmatalesSpiroplasmataceaeSpiroplasma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 749749Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolasePRO_0000166575Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO34098.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 148100HDAdd
BLAST
Domaini674 – 74976ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RelA/SpoT family.Curated
Contains 1 ACT domain.PROSITE-ProRule annotation
Contains 1 HD domain.Curated

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR002912. 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]
PfamiPF01842. ACT. 1 hit.
PF01966. HD. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
SM00954. RelA_SpoT. 1 hit.
[Graphical view]
SUPFAMiSSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00691. spoT_relA. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34098-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRDIKYEEV LAQIKLYIKD EATLKEIQKA YEYAEEKHHG QVRNSGARYI
60 70 80 90 100
IHPLWTTFFL AQWRMGPKTL IAGLLHDVLE DTPATFEELQ ELFGIEIANL
110 120 130 140 150
VEGVTKVSYF AKENRTQIKA QYLRKLYLSM AKDIRVIIVK LADRLHNLKT
160 170 180 190 200
IGYLKPERQQ IIARESLEIY SAIAHRLGMK AVKQEIEDIS FKIINPVQYN
210 220 230 240 250
KIVSLLESSN KERENTINQK IEELKKILIT EKKMSVKVYG RSKSIYSIYR
260 270 280 290 300
KMNQFGKNFD DIHDILAVRI ITNSVDDCYK VLGFVHQHYT PLNNRFKDYI
310 320 330 340 350
ATPKHNLYQS LHTTIVADDG LIFEVQIRTE EMDELAEQGV AAHWRYKEGE
360 370 380 390 400
NYDIAKKQKD IDERLDIFKR ILDLENISVQ ERDEIQQEVY KPDHLMEQII
410 420 430 440 450
QNDIFSSLIY VLTPNGKVVT LPFGSTVLDF AYKIHSEIGE KTIGAKINGL
460 470 480 490 500
FSPISTVLKS GDVVDIKTAA TQKPNHSWLV VSKTSSALEK IKKYLKKELV
510 520 530 540 550
EVTSDAKSVN LEKIKQTKSQ IEEYIAKKDL KWKLVNSETQ LERLHAINFN
560 570 580 590 600
NIEDFLLDVA NDEYTLEEAI NLVYLDHETS QNEKILKKLQ DKQYKKAQLK
610 620 630 640 650
DDIIVQGISN IKVVISQCCL PIPYEDITGY VSKAEGIKVH LKTCRNIQSG
660 670 680 690 700
DKQDRQVEVS WNEAVCKNKQ YDCAIRIEAI DRPALLVDVT KVLSHLNASV
710 720 730 740
QMMSANVSGD LMNLTIKTII KVSNADRLQQ IRSSLLTIPD IKVVERVMM
Length:749
Mass (Da):86,282
Last modified:January 1, 1998 - v1
Checksum:iD32992E612317042
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89875 Genomic DNA. Translation: AAC45548.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89875 Genomic DNA. Translation: AAC45548.1.

3D structure databases

ProteinModelPortaliO34098.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00908; UER00886.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR002912. 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]
PfamiPF01842. ACT. 1 hit.
PF01966. HD. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
SM00954. RelA_SpoT. 1 hit.
[Graphical view]
SUPFAMiSSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00691. spoT_relA. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiSPOT_SPICI
AccessioniPrimary (citable) accession number: O34098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.