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Reviewed, UniProtKB/Swiss-Prot Q2IH81 (PYRG_ANADE)

Last modified June 16, 2009. Version 27. 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: Adeh_4174
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length555 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 – 555555CTP synthase HAMAP MF_01227
PRO_0000266053

Regions

Domain297 – 537241Glutamine amidotransferase type-1
Region1 – 258258Aminator domain HAMAP MF_01227

Sites

Active site3851Nucleophile By similarity
Active site5101 By similarity
Active site5121 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IH81-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 27D67205E2F1C146

FASTA55561,367
        10         20         30         40         50         60 
MVKRGKKTKY LFVTGGVVSS LGKGLSAASI GALLENRGLE VQHLKLDPYI NVDPGTMSPF 

        70         80         90        100        110        120 
QHGEVFVTDD GAETDLDLGH YERFTSAKMT RRNNYTTGRI YQNVIQRERR GEYLGKTVQV 

       130        140        150        160        170        180 
IPHITDEIKA VIREAAGGAD ILIVEVGGTV GDIESLPFLE AIRQMKYDVG EENAVYAHLT 

       190        200        210        220        230        240 
LVPFIAAAGE LKTKPTQHSV KELREIGIQP DLLLCRSDRE IPRDMKDKIA LFCNVDPSAV 

       250        260        270        280        290        300 
FTALDVPSIY EVPLSLHREG LDDKLAELFN IWSRAPRLER WETIVDKVKN PRRGEVRIGI 

       310        320        330        340        350        360 
VGKYVELHES YKSLNEALVH GGIANDARVK LAFIDSTKLE EGDLSDLDKV DAILVPGGFG 

       370        380        390        400        410        420 
IRGTEGKILG VKYAREHKVP FFGICLGLQM AVIEMARNVL GLAGANSLEF DEQTPHPVVT 

       430        440        450        460        470        480 
LMEGQKGVTD KGGTMRLGAY PCALKEGTKA RALYGADLVH ERHRHRFEFN NDYRAQFEAA 

       490        500        510        520        530        540 
GMVFSGVNPD LGLVEMIELP GQHFVGCQFH PEFRSKPFAP HPLFAGFVKA ALEHRDAQQR 

       550 
QPSAEVKKLP VGKNG 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000251 Genomic DNA. Translation: ABC83938.1.
RefSeqYP_467375.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3887994.
GenomeReviewsGene locus Adeh_4174 in contig CP000251_GR.
KEGGade:Adeh_4174.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2IH81.
OMAQ2IH81. EFNNAYR.

Enzyme and pathway databases

BioCycADEH290397:ADEH_4174-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_ANADE
AccessionPrimary (citable) accession number: Q2IH81
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 7, 2006
Last modified: June 16, 2009
This is version 27 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