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Reviewed, UniProtKB/Swiss-Prot Q5PBX6 (PYRG_ANAMM)

Last modified June 16, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    CTP synthase
    EC=6.3.4.2
Alternative name(s):
    UTP--ammonia ligase
    CTP synthetase
Gene names
Name: pyrG
Ordered Locus Names: AM018
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen By similarity.

Catalytic activity

ATP + UTP + NH3 = ADP + phosphate + CTP. HAMAP MF_01227

Enzyme regulation

Allosterically activated by GTP, when glutamine is the substrate. Inhibited by CTP By similarity.

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. HAMAP MF_01227

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the CTP synthase family.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 560560CTP synthase HAMAP MF_01227
PRO_0000266054

Regions

Domain297 – 539243Glutamine amidotransferase type-1
Region1 – 259259Aminator domain HAMAP MF_01227

Sites

Active site3831Nucleophile By similarity
Active site5121 By similarity
Active site5141 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PBX6-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: D64F80BDE27F74D2

FASTA56061,146
        10         20         30         40         50         60 
MSIRDGCSAR FIFVTGGVVS SLGKGLAAAS IGALLQARGF RVRLRKLDPY LNVDPGTMSP 

        70         80         90        100        110        120 
AQHGEVFVTD DGGETDLDLG NYERFTGVNT TKEDNITAGR IYQQLLAKER RGDYLGHTVQ 

       130        140        150        160        170        180 
VIPHVTDLII SFILSNDDGA DFIICEIGGT VGDIESQPFL ESIRQVSYRL SKNFTIFVHL 

       190        200        210        220        230        240 
TLVPCVGSAG ELKTKPTQHS VKELSSLGIQ PDIILYRSAE PLPQYQSAKI ANFCNVSADN 

       250        260        270        280        290        300 
VIPALDVESM YKLPVMYHAH KLDTQILSHF GMGAPEPDLT KWANVLTMVN NARNVVTIAI 

       310        320        330        340        350        360 
IGKYTKFLDA YTSLTEALDH AGMHSGIKIQ VKWVDSRLPV RESDLHDVDG VLIPGGFGDD 

       370        380        390        400        410        420 
GVDGKVLAIG YARANGIPML GICMGMQLAA IEFALNVAKL EDANSTEFNQ ACKNPIVVEL 

       430        440        450        460        470        480 
PWLQKGEGEY LLGGSMRLGS CTYRLSADSR VASVYGSTVI NERCRHRYCI NPQYKNVLEE 

       490        500        510        520        530        540 
HGLSFTGMSD SHGLVEVLEL QSHPWFIGVQ FHPEFKSSPF APHPLFTSFV QNVLQIKQRG 

       550        560 
FMHKSVSAAA ILVPGSSVVS 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000030 Genomic DNA. Translation: AAV86203.1.
RefSeqYP_153458.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3171313.
GenomeReviewsGene locus AM018 in contig CP000030_GR.
KEGGama:AM018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PBX6.
OMAQ5PBX6. EFNNAYR.

Enzyme and pathway databases

BioCycAMAR234826:AM018-MON.

Family and domain databases

HAMAPMF_01227.
[Tree]
InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
[Graphical view]
PANTHERPTHR11550. PyrG_synth. 1 hit.
PfamPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00337. PyrG. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRG_ANAMM
AccessionPrimary (citable) accession number: Q5PBX6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents