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P51039

- CISY_RICAU

UniProt

P51039 - CISY_RICAU

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Protein
Citrate synthase
Gene
gltA
Organism
Rickettsia australis
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei304 – 3041 By similarity
Active sitei363 – 3631 By similarity

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: InterPro

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 (EC:2.3.3.16)
Gene namesi
Name:gltA
OrganismiRickettsia australis
Taxonomic identifieri787 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›411›411Citrate synthase
PRO_0000169958Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP51039.
SMRiP51039. Positions 5-411.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. 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.
IPR010953. Citrate_synthase_typ-I.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01798. cit_synth_I. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P51039-1 [UniParc]FASTAAdd to Basket

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DSEFAELKIR GKIFKLPILK ASIGEDVIDI SRVSAEADCF TYDPGFMSTA    50
SCQSTITYID GDKGILRHRG YNIKDLAEKS DFLEVAYLLI YGELPTIEQY 100
NNFTTQVAHH SLVNERLHYL FQAFCSSSHP MAIMLAAVGS LSAFYPDLLN 150
FKEADYELTA IRMIAKIPTI AAMSYKYSIG QPFIYPDNSL DFTENFLHMM 200
FATPCTKYKV NPIIKNALNK IFILHADHEQ NASTSTVRIA GSSGANAFAC 250
ISTGIASLWG PAHGGANEAV INMLKEIGSS ENIPKFIAKA KDKNDPFRLM 300
GFGHRVYKNY DPRAAVLKET CKAVLKELGQ LENNPLLQIA IELEAIALKD 350
EYFIERKLYP NVDFYSGIIY KAMGIPSQMF TVLFAIARTV GWMAQWKEMH 400
EDPEQKISRP R 411
Length:411
Mass (Da):46,112
Last modified:November 1, 1997 - v2
Checksum:i9D0571AFD3B6B27D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti290 – 2901A → V in AAB49576. 1 Publication
Sequence conflicti316 – 3161V → A in AAB49576. 1 Publication
Sequence conflicti364 – 3652FY → SH in AAB49576. 1 Publication
Sequence conflicti380 – 3801F → S in AAB49576. 1 Publication

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei411 – 4111

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59718 Genomic DNA. Translation: AAB02954.1.
U33923 Genomic DNA. Translation: AAB49576.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59718 Genomic DNA. Translation: AAB02954.1 .
U33923 Genomic DNA. Translation: AAB49576.1 .

3D structure databases

ProteinModelPortali P51039.
SMRi P51039. Positions 5-411.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProi 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.
IPR010953. Citrate_synthase_typ-I.
[Graphical view ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PIRSFi PIRSF001369. Citrate_synth. 1 hit.
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
TIGRFAMsi TIGR01798. cit_synth_I. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Citrate synthase gene comparison, a new tool for phylogenetic analysis, and its application for the rickettsiae."
    Roux V., Rydkina E., Eremeeva M., Raoult D.
    Int. J. Syst. Bacteriol. 47:252-261(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Phillips.
  2. Higgins J.A., Radulovic S., Schriefer M.E.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-383.
    Strain: JC.

Entry informationi

Entry nameiCISY_RICAU
AccessioniPrimary (citable) accession number: P51039
Secondary accession number(s): Q59731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Documents

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

External Data

Dasty 3

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