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Protein

Citrate synthase

Gene

gltA

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect (By similarity).By similarity

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotationBy similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei220 – 2201PROSITE-ProRule annotation
Active sitei259 – 2591PROSITE-ProRule annotation
Active sitei313 – 3131PROSITE-ProRule annotation

GO - Molecular functioni

  1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer 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

BioCyciDRAD243230:GH46-779-MONOMER.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
Ordered Locus Names:DR_0757
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 377376Citrate synthasePRO_0000169942Add
BLAST

Proteomic databases

PRIDEiQ9RWB2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi243230.DR_0757.

Structurei

3D structure databases

ProteinModelPortaliQ9RWB2.
SMRiQ9RWB2. Positions 4-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiQ9RWB2.
KOiK01647.
OMAiDNRLLRP.
OrthoDBiEOG6P8TP4.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
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]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9RWB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNIAKGLEG VLFTESKLTF INGSEGILTH LGIPIQEWAE KSTFEELSLA
60 70 80 90 100
LLDAKLPTAE ELAKFDAELK ANRAIPDQLV GIIRDMPKGV HPMQALRTAV
110 120 130 140 150
SYLGLLDPQA EDITPEARRA ISTRMIAQFS TIIAAINRAQ EGQDIVAPRA
160 170 180 190 200
DLTHAGNFLY MLTGNEPTPE QARLFDIALV LHADHGMNAS TFTAIATSST
210 220 230 240 250
LSDMYSCMVS AIGALKGPLH GGANEAVMTM LDEIGTVDKA EAYITGKLDN
260 270 280 290 300
KEKIMGVGHR VYKYFDPRSR VLRDYAEHVA NKEGKSNYYQ ILEAIEKIIV
310 320 330 340 350
DRMGAKGIYP NVDFYSGTVY SDLGIKKEYF TPIFALARIS GWCASVIEYS
360 370
QDNRLLRPDA EYTGARDQHY VDIKDRQ
Length:377
Mass (Da):41,628
Last modified:January 22, 2007 - v3
Checksum:i268F74D5B8EC37DA
GO

Sequence cautioni

The sequence AAF10336.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10336.1. Different initiation.
PIRiA75479.
RefSeqiNP_294481.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF10336; AAF10336; DR_0757.
GeneIDi1798731.
KEGGidra:DR_0757.
PATRICi21629062. VBIDeiRad64572_0937.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10336.1. Different initiation.
PIRiA75479.
RefSeqiNP_294481.1. NC_001263.1.

3D structure databases

ProteinModelPortaliQ9RWB2.
SMRiQ9RWB2. Positions 4-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0757.

Proteomic databases

PRIDEiQ9RWB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF10336; AAF10336; DR_0757.
GeneIDi1798731.
KEGGidra:DR_0757.
PATRICi21629062. VBIDeiRad64572_0937.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiQ9RWB2.
KOiK01647.
OMAiDNRLLRP.
OrthoDBiEOG6P8TP4.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciDRAD243230:GH46-779-MONOMER.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
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]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  2. "Protein recycling is a major component of post-irradiation recovery in Deinococcus radiodurans strain R1."
    Joshi B.S., Schmid R., Altendorf K., Apte S.K.
    Biochem. Biophys. Res. Commun. 320:1112-1117(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-14.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiCISY_DEIRA
AccessioniPrimary (citable) accession number: Q9RWB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 29, 2004
Last sequence update: January 22, 2007
Last modified: January 6, 2015
This is version 93 of the entry and version 3 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.By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.