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P49299 (CYSZ_CUCMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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, glyoxysomal

EC=2.3.3.1
Alternative name(s):
GCS
OrganismCucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifier3661 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subcellular location

Glyoxysome.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentGlyoxysome
Peroxisome
   DomainTransit peptide
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentglyoxysome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncitrate (Si)-synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Glyoxysome Ref.1
Chain44 – 516473Citrate synthase, glyoxysomal
PRO_0000005490

Sites

Active site3291 By similarity
Active site3681 By similarity
Active site4241 By similarity

Sequences

Sequence LengthMass (Da)Tools
P49299 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 162F6270284A3F6B

FASTA51656,759
        10         20         30         40         50         60 
MPTDMELSPS NVARHRLAVL AAHLSAASLE PPVMASSLEA HCVSAQTMVA PPELVKGTLT 

        70         80         90        100        110        120 
IVDERTGKRY QVQVSEEGTI KATDLKKITT GPNDKGLKLY DPGYLNTAPV RSSISYIDGD 

       130        140        150        160        170        180 
LGILRYRGYP IEELAESSTY VEVAYLLMYG NLPSQSQLAD WEFAISQHSA VPQGLVDIIQ 

       190        200        210        220        230        240 
AMPHDAHPMG VLVSAMSALS VFHPDANPAL RGQDLYKSKQ VRDKQIARII GKAPTIAAAA 

       250        260        270        280        290        300 
YLRLAGRPPV LPSSNLSYSE NFLYMLDSLG NRSYKPNPRL ARVLDILFIL HAEHEMNCST 

       310        320        330        340        350        360 
SAARHLASSG VDVFTALSGA VGALYGPLHG GANEAVLKML SEIGTVNNIP EFIEGVKNRK 

       370        380        390        400        410        420 
RKMSGFGHRV YKNYDPRAKV IRKLAEEVFS IVGRDPLIEV AVALEKAALS DEYFVKRKLY 

       430        440        450        460        470        480 
PNVDFYSGLI YRAMGFPPEF FTVLFAIPRM AGYLAHWRES LDDPDTKIIR PQQVYTGEWL 

       490        500        510 
RHYIPPNERL VPAKADRLGQ VSVSNASKRR LSGSGI 

« Hide

References

[1]"Molecular characterization of a glyoxysomal citrate synthase that is synthesized as a precursor of higher molecular mass in pumpkin."
Kato A., Hayashi M., Mori H., Nishimura M.
Plant Mol. Biol. 27:377-390(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-51.
Strain: cv. Kurokawa Amakuri Nankin.
Tissue: Etiolated cotyledon.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38132 mRNA. Translation: BAA07328.1.
PIRS53008.

3D structure databases

ProteinModelPortalP49299.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP49299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00703; UER00717.

Family and domain databases

Gene3D1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProIPR016142. 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.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSZ_CUCMA
AccessionPrimary (citable) accession number: P49299
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways