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P80148

- CISY_SULSO

UniProt

P80148 - CISY_SULSO

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Protein

Citrate synthase

Gene

gltA

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Enzyme regulationi

Allosterically inhibited by NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei258 – 2581PROSITE-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

BioCyciSSOL273057:GCH2-2399-MONOMER.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
Ordered Locus Names:SSO2589
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Citrate synthasePRO_0000169977Add
BLAST

Post-translational modificationi

The N-terminus is blocked by acetylation.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP80148.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi273057.SSO2589.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83
Beta strandi12 – 2211
Turni23 – 264
Beta strandi27 – 304
Helixi35 – 417
Helixi44 – 5310
Helixi59 – 7012
Helixi77 – 859
Helixi92 – 10615
Beta strandi112 – 1154
Helixi116 – 13823
Helixi152 – 16110
Helixi167 – 18014
Helixi187 – 19711
Helixi202 – 21312
Turni216 – 2205
Helixi221 – 23212
Helixi235 – 2373
Helixi238 – 2458
Turni246 – 2494
Helixi266 – 27914
Helixi283 – 30321
Turni304 – 3074
Turni312 – 3154
Helixi316 – 3238
Helixi327 – 3293
Helixi330 – 35223
Beta strandi360 – 3634

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O7XX-ray2.70A/B/C/D1-377[»]
ProteinModelPortaliP80148.
SMRiP80148. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80148.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiP80148.
KOiK01647.
OMAiIDHEANA.

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.

P80148-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVVSKGLEN VIIKVTNLTF IDGEKGILRY RGYNIEDLVN YGSYEETIYL
60 70 80 90 100
MLYGKLPTKK ELNDLKAKLN EEYEVPQEVL DTIYLMPKEA DAIGLLEVGT
110 120 130 140 150
AALASIDKNF KWKENDKEKA ISIIAKMATL VANVYRRKEG NKPRIPEPSD
160 170 180 190 200
SFAKSFLLAS FAREPTTDEI NAMDKALILY TDHEVPASTT AALVAASTLS
210 220 230 240 250
DMYSSLTAAL AALKGPLHGG AAEEAFKQFI EIGDPNRVQN WFNDKVVNQK
260 270 280 290 300
NRLMGFGHRV YKTYDPRAKI FKKLALTLIE RNADARRYFE IAQKLEELGI
310 320 330 340 350
KQFSSKGIYP NTDFYSGIVF YALGFPVYMF TALFALSRTL GWLAHIIEYV
360 370
EEQHRLIRPR ALYVGPEYQE YVSIDKR
Length:377
Mass (Da):42,752
Last modified:June 1, 2001 - v3
Checksum:iE3036E232F134F11
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101N → D AA sequence (PubMed:1521537)Curated
Sequence conflicti12 – 121I → Y AA sequence (PubMed:1521537)Curated
Sequence conflicti15 – 151V → S AA sequence (PubMed:1521537)Curated
Sequence conflicti17 – 171N → S AA sequence (PubMed:1521537)Curated
Sequence conflicti20 – 201F → Y AA sequence (PubMed:1521537)Curated
Sequence conflicti24 – 252EK → VN AA sequence (PubMed:1521537)Curated
Sequence conflicti27 – 271I → V AA sequence (PubMed:1521537)Curated
Sequence conflicti57 – 571P → R in AAB09594. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70879 Genomic DNA. Translation: AAB09594.1.
AE006641 Genomic DNA. Translation: AAK42713.1.
PIRiB90432.
RefSeqiNP_343923.1. NC_002754.1.
WP_009989299.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK42713; AAK42713; SSO2589.
GeneIDi1454040.
KEGGisso:SSO2589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U70879 Genomic DNA. Translation: AAB09594.1 .
AE006641 Genomic DNA. Translation: AAK42713.1 .
PIRi B90432.
RefSeqi NP_343923.1. NC_002754.1.
WP_009989299.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O7X X-ray 2.70 A/B/C/D 1-377 [» ]
ProteinModelPortali P80148.
SMRi P80148. Positions 3-372.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273057.SSO2589.

Proteomic databases

PRIDEi P80148.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK42713 ; AAK42713 ; SSO2589 .
GeneIDi 1454040.
KEGGi sso:SSO2589.

Phylogenomic databases

eggNOGi COG0372.
HOGENOMi HOG000021225.
InParanoidi P80148.
KOi K01647.
OMAi IDHEANA.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .
BioCyci SSOL273057:GCH2-2399-MONOMER.

Miscellaneous databases

EvolutionaryTracei P80148.

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProi IPR011278. 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 ]
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 TIGR01800. cit_synth_II. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sulfolobus solfataricus citrate synthase."
    Connaris H., Danson M.J., Hough D.W.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase."
    Lill U., Lefrank S., Henschen A., Eggerer H.
    Eur. J. Biochem. 208:459-466(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-30, ACETYLATION.

Entry informationi

Entry nameiCISY_SULSO
AccessioniPrimary (citable) accession number: P80148
Secondary accession number(s): P77979
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 108 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.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3