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O34002

- CISY_ABDS2

UniProt

O34002 - CISY_ABDS2

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Protein

Citrate synthase

Gene

gltA

Organism
Antarctic bacterium DS2-3R
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

Temperature dependencei

Optimum temperature is 31 degrees Celsius. Cold-active. Is rapidly inactivated at 45 degrees Celsius, and shows significant activity at 10 degrees Celsius and below.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei270 – 2701PROSITE-ProRule annotation
Active sitei321 – 3211PROSITE-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

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
Synonyms:cisY
OrganismiAntarctic bacterium DS2-3R
Taxonomic identifieri56673 [NCBI]
Taxonomic lineageiBacteria

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Citrate synthasePRO_0000169925Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Beta strandi19 – 246Combined sources
Turni25 – 284Combined sources
Beta strandi29 – 324Combined sources
Helixi37 – 437Combined sources
Helixi46 – 5510Combined sources
Helixi61 – 7212Combined sources
Helixi79 – 857Combined sources
Helixi94 – 10714Combined sources
Turni110 – 1134Combined sources
Helixi117 – 14226Combined sources
Helixi156 – 16510Combined sources
Helixi171 – 18414Combined sources
Helixi191 – 20010Combined sources
Turni201 – 2033Combined sources
Helixi206 – 21813Combined sources
Turni220 – 2245Combined sources
Helixi225 – 23511Combined sources
Helixi244 – 26017Combined sources
Helixi280 – 29314Combined sources
Helixi298 – 31417Combined sources
Helixi321 – 33010Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 35922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A59X-ray2.09A2-379[»]
ProteinModelPortaliO34002.
SMRiO34002. Positions 3-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34002.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

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.

O34002-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEPTIHKGL AGVTADVTAI SKVNSDTNSL LYRGYPVQEL AAKCSFEQVA
60 70 80 90 100
YLLWNSELPN DSELKAFVNF ERSHRKLDEN VKGAIDLLST ACHPMDVART
110 120 130 140 150
AVSVLGANHA RAQDSSPEAN LEKAMSLLAT FPSVVAYDQR RRRGEELIEP
160 170 180 190 200
REDLDYSANF LWMTFGEEAA PEVVEAFNVS MILYAEHSFN ASTFTARVIT
210 220 230 240 250
STLADLHSAV TGAIGALKGP LHGGANEAVM HTFEEIGIRK DESLDEAATR
260 270 280 290 300
SKAWMVDALA QKKKVMGFGH RVYKNGDSRV PTMKSALDAM IKHYDRPEML
310 320 330 340 350
GLYNGLEAAM EEAKQIKPNL DYPAGPTYNL MGFDTEMFTP LFIAARITGW
360 370
TAHIMEQVAD NALIRPLSEY NGPEQRQVP
Length:379
Mass (Da):41,832
Last modified:January 1, 1998 - v1
Checksum:i7D8F4614E3D1CC9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85944 Genomic DNA. Translation: AAC45662.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85944 Genomic DNA. Translation: AAC45662.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A59 X-ray 2.09 A 2-379 [» ]
ProteinModelPortali O34002.
SMRi O34002. Positions 3-379.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .

Miscellaneous databases

EvolutionaryTracei O34002.

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

  1. "Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R."
    Gerike U., Danson M.J., Russell N.J., Hough D.W.
    Eur. J. Biochem. 248:49-57(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium."
    Russell R.J., Gerike U., Danson M.J., Hough D.W., Taylor G.L.
    Structure 6:351-361(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).

Entry informationi

Entry nameiCISY_ABDS2
AccessioniPrimary (citable) accession number: O34002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 75 of the entry and version 1 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

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