gltA:Gene Product(s)

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

GltA product

Synonyms

citrate synthase product[1], B0720 product[2][1], IcdB product[2][1], GltA product[2][1]

Product description

citrate synthase monomer[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0003824

catalytic activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0021

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0006099

tricarboxylic acid cycle

PMID:13152052[5]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc 11.1[3].

complete

GO:0009061

anaerobic respiration

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0003878

ATP citrate synthase activity

F

required field missing

GO:0004108

citrate (Si)-synthase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010953

F

Seeded from EcoCyc 12.5 [4]

complete

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Interactions

Partner Type Partner Notes
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Notes

Localization

Compartment Description Evidence Notes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc 

MADTKAKLTL NGDTAVELDV LKGTLGQDVI DIRTLGSKGV FTFDPGFTST ASCESKITFI
DGDEGILLHR GFPIDQLATD SNYLEVCYIL LNGEKPTQEQ YDEFKTTVTR HTMIHEQITR
LFHAFRRDSH PMAVMCGITG ALAAFYHDSL DVNNPRHREI AAFRLLSKMP TMAAMCYKYS
IGQPFVYPRN DLSYAGNFLN MMFSTPCEPY EVNPILERAM DRILILHADH EQNASTSTVR
TAGSSGANPF ACIAAGIASL WGPAHGGANE AALKMLEEIS SVKHIPEFVR RAKDKNDSFR
LMGFGHRVYK NYDPRATVMR ETCHEVLKEL GTKDDLLEVA MELENIALND PYFIEKKLYP
NVDFYSGIIL KAMGIPSSMF TVIFAMARTV GWIAHWSEMH SDGMKIARPR QLYTGYEKRD
FKSDIKR
Mol. Wt

48.01 kDa (calc) [2]

pI

6.62[2]

Extinction coefficient

40340 - 41215 (calc based on 16 Y, 3 W, and 7 C residues)

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Domains/Motifs/Modification Sites

Type Residues Description Notes
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Structure

Structure Type Organism Accession Residues covered Notes

X-RAY DIFFRACTION

Escherichia coli

1OWC Three Dimensional Structure Analysis Of The R109L Variant of the Type II Citrate Synthase From E. Coli

X-RAY DIFFRACTION

Escherichia coli

1OWB Three Dimensional Structure Analysis Of The Variant R109L NADH Complex of Type II Citrate Synthase From E. Coli

X-RAY DIFFRACTION

Escherichia coli

1NXG The F383A variant of type II Citrate Synthase complexed with NADH

X-RAY DIFFRACTION

Escherichia coli

1NXE A Novel NADH Allosteric Regulator Site is Found on the Surface of the Hexameric Type II Phe383Ala Variant of Citrate Synthase

X-RAY DIFFRACTION

Escherichia coli

1K3P Three Dimensional Structure Analysis of the Type II Citrate Synthase from E.coli

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Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:CITSYN-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0ABH7

PFAM (EcoliWiki Page)

PFAM:PF00285

RefSeq (EcoliWiki Page)

RefSeq:NP_415248

ModBase (EcoliWiki Page)

ModBase:P0ABH7

PDB (EcoliWiki Page)

PDB:1K3P

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Notes

Links

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Name URL Comments
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References

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  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.0 4.1 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. ↑ SWIM, HE & KRAMPITZ, LO (1954) Acetic acid oxidation by Escherichia coli; evidence for the occurrence of a tricarboxylic acid cycle. J. Bacteriol. 67 419-25 PubMed


Categories

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