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P51044 (CISY_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, mitochondrial

EC=2.3.3.16
Gene names
Name:cit-1
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subcellular location

Mitochondrion matrix By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncitrate (Si)-synthase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion By similarity
Chain? – 475Citrate synthase, mitochondrialPRO_0000005475

Sites

Active site3101 By similarity
Active site3561 By similarity
Active site4111 By similarity

Sequences

Sequence LengthMass (Da)Tools
P51044 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F93525B3F31FCB3F

FASTA47552,154
        10         20         30         40         50         60 
MASTLRLGTS ALRSSSIAAK PVVQSAAFNG LRCYSTGKAK SLKETFAEKL PAELEKVKKL 

        70         80         90        100        110        120 
RKEHGSKVIG EVTLDQAYGG ARGVKCLVWE GSVLDSEEGI RFRGRTIPEC QELLPKAPGG 

       130        140        150        160        170        180 
QEPLPEGLFW LLLTGEIPTE QQVRDLSAEW AARSDLPKFI EELIDRCPST LHPMSQFSLA 

       190        200        210        220        230        240 
VTALEHESAF AKAYAKGINK KDYWNYTFED SMDLIAKLPT IAAKIYRNVF KDGKVAPIQK 

       250        260        270        280        290        300 
DKDYSYNLAN QLGYGDNNDF VELMRLYLTI HSDHEGGNVS AHTTHLVGSA LSSPMLSLAA 

       310        320        330        340        350        360 
GLNGLAGPLH GLANQEVLNW LTKMKAAIGN DLSDEAIKNY LWSTLNAGQV VPGYGHAVLR 

       370        380        390        400        410        420 
KTDPRYVSQR EFALRKLPDD PMFKLVSQVY KIAPGVLTEH GKTKNPYPNV DAHSGVLLQY 

       430        440        450        460        470 
YGLTEANYYT VLFGVSRALG VLPQLIIDRA LGAPIERPKS YSTELSPSLL VLSCK 

« Hide

References

[1]"Cloning and expression of cDNA encoding Aspergillus niger citrate synthase in Esherichia coli."
Oshida Y., Miyake K., Kanayama S., Kirimura K., Usami S.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: WU-2223L.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63376 mRNA. Translation: BAA09691.1.

3D structure databases

ProteinModelPortalP51044.
SMRP51044. Positions 39-464.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP51044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0372.

Enzyme and pathway databases

UniPathwayUPA00223; UER00717.

Family and domain databases

Gene3D1.10.580.10. 1 hit.
InterProIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
TIGRFAMsTIGR01793. cit_synth_euk. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCISY_ASPNG
AccessionPrimary (citable) accession number: P51044
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways