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P80148 (CISY_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Citrate synthase

EC=2.3.3.1
Gene names
Name:gltA
Ordered Locus Names:SSO2589
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Enzyme regulation

Allosterically inhibited by NADH.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.

Subunit structure

Homodimer.

Post-translational modification

The N-terminus is blocked by acetylation. Ref.3

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

Sequence similarities

Belongs to the citrate synthase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Citrate synthase
PRO_0000169977

Sites

Active site2581 By similarity
Active site3131 By similarity

Experimental info

Sequence conflict101N → D AA sequence Ref.3
Sequence conflict121I → Y AA sequence Ref.3
Sequence conflict151V → S AA sequence Ref.3
Sequence conflict171N → S AA sequence Ref.3
Sequence conflict201F → Y AA sequence Ref.3
Sequence conflict24 – 252EK → VN AA sequence Ref.3
Sequence conflict271I → V AA sequence Ref.3
Sequence conflict571P → R in AAB09594. Ref.1

Secondary structure

................................................ 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80148 [UniParc].

Last modified June 1, 2001. Version 3.
Checksum: E3036E232F134F11

FASTA37742,752
        10         20         30         40         50         60 
MSVVSKGLEN VIIKVTNLTF IDGEKGILRY RGYNIEDLVN YGSYEETIYL MLYGKLPTKK 

        70         80         90        100        110        120 
ELNDLKAKLN EEYEVPQEVL DTIYLMPKEA DAIGLLEVGT AALASIDKNF KWKENDKEKA 

       130        140        150        160        170        180 
ISIIAKMATL VANVYRRKEG NKPRIPEPSD SFAKSFLLAS FAREPTTDEI NAMDKALILY 

       190        200        210        220        230        240 
TDHEVPASTT AALVAASTLS DMYSSLTAAL AALKGPLHGG AAEEAFKQFI EIGDPNRVQN 

       250        260        270        280        290        300 
WFNDKVVNQK NRLMGFGHRV YKTYDPRAKI FKKLALTLIE RNADARRYFE IAQKLEELGI 

       310        320        330        340        350        360 
KQFSSKGIYP NTDFYSGIVF YALGFPVYMF TALFALSRTL GWLAHIIEYV EEQHRLIRPR 

       370 
ALYVGPEYQE YVSIDKR 

« Hide

References

« Hide 'large scale' references
[1]"Sulfolobus solfataricus citrate synthase."
Connaris H., Danson M.J., Hough D.W.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.
[2]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]"Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase."
Lill U., Lefrank S., Henschen A., Eggerer H.
Eur. J. Biochem. 208:459-466(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 7-30, ACETYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70879 Genomic DNA. Translation: AAB09594.1.
AE006641 Genomic DNA. Translation: AAK42713.1.
PIRB90432.
RefSeqNP_343923.1. NC_002754.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1O7XX-ray2.70A/B/C/D1-377[»]
ProteinModelPortalP80148.
SMRP80148. Positions 3-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273057.SSO2589.

Proteomic databases

PRIDEP80148.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK42713; AAK42713; SSO2589.
GeneID1454040.
KEGGsso:SSO2589.

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000021225.
KOK01647.
OMANKEDGVR.
ProtClustDBPRK14037.

Enzyme and pathway databases

BioCycSSOL273057:GCH2-2399-MONOMER.
UniPathwayUPA00223; UER00717.

Family and domain databases

Gene3D1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProIPR011278. 2-MeCitrate/Citrate_synth_I.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFPIRSF001369. Citrate_synth. 1 hit.
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
TIGRFAMsTIGR01800. cit_synth_II. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80148.

Entry information

Entry nameCISY_SULSO
AccessionPrimary (citable) accession number: P80148
Secondary accession number(s): P77979
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 2001
Last modified: October 16, 2013
This is version 103 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways