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Q0QEL7

- CISY_MESAU

UniProt

Q0QEL7 - CISY_MESAU

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Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.By similarityPROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741By similarityPROSITE-ProRule annotation
Active sitei120 – 1201By similarityPROSITE-ProRule annotation
Active sitei175 – 1751By similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrialBy similarity (EC:2.3.3.1)
Alternative name(s):
Citrate (Si)-synthase
Gene namesi
Name:CSImported
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›213›213Citrate synthase, mitochondrialPRO_0000394310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941N6-acetyllysine; alternateBy similarity
Modified residuei94 – 941N6-succinyllysine; alternateBy similarity
Modified residuei100 – 1001N6-acetyllysine; alternateBy similarity
Modified residuei100 – 1001N6-succinyllysine; alternateBy similarity
Modified residuei148 – 1481N6-acetyllysine; alternateBy similarity
Modified residuei148 – 1481N6-succinyllysine; alternateBy similarity
Modified residuei155 – 1551N6-acetyllysineBy similarity
Modified residuei166 – 1661N6-acetyllysine; alternateBy similarity
Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
Modified residuei168 – 1681N6,N6,N6-trimethyllysineBy similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PRIDEiQ0QEL7.

Interactioni

Subunit structurei

Homodimer.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Sequence Analysis

Phylogenomic databases

HOVERGENiHBG005336.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q0QEL7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
GAIDSKLDWS HNFTNMLGYT EPQFTELMRL YLTIHSDHEG GNVSAHTSHL
60 70 80 90 100
VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLVWLTQLQK EVGKDVSDEK
110 120 130 140 150
LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY SCQREFALKH LPNDPLFKLV
160 170 180 190 200
AQLYKIVPNI LLEQGKAKNP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS
210
RALGVLAQLI WSR
Length:213
Mass (Da):23,884
Last modified:September 5, 2006 - v1
Checksum:iF423CBF73DF89D63
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported
Non-terminal residuei213 – 2131Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ403127 mRNA. Translation: ABD77260.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ403127 mRNA. Translation: ABD77260.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q0QEL7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005336.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .

Family and domain databases

Gene3Di 1.10.580.10. 1 hit.
InterProi IPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
[Graphical view ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
    Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
    Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: LiverImported.
  2. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
    Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
    Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCISY_MESAU
AccessioniPrimary (citable) accession number: Q0QEL7
Secondary accession number(s): P86224
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: September 5, 2006
Last modified: October 29, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Documents

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

External Data

Dasty 3