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InterPro: IPR011206 Citrate lyase, beta subunit

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UniProtKB

Matches:

1366 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR011206 Citrate_lyase_beta

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF015582	Cit_lyase_B	1366
Signatures in BioMart

InterPro Relationships Help

Parent

IPR005000 HpcH/HpaI aldolase

Children

IPR006475 Citrate lyase, beta subunit, bacteria

Contains

IPR015813 Pyruvate/Phosphoenolpyruvate kinase, catalytic core

GO Term annotation Help

Function

GO:0008815 citrate (pro-3S)-lyase activity

Component

GO:0009346 citrate lyase complex

InterPro annotation

Entry Details in BioMart

Abstract

Citrate lyase catalyses the magnesium-dependent cleavage of citrate to acetate and oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The bacterial enzyme is composed of three subunits: alpha, beta and gamma. Catalytic activity resides on the alpha- and beta-subunits, whereas the gamma-subunit serves as an acyl carrier protein (ACP) [1]. Mammalian citrate lyase beta proteins display similarity to the bacterial enzymes [2].

Structural links Help

PDB - click here

SCOP: c.1.12.5

CATH: 3.20.20.60

Database links Help

Enzyme: EC:4.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011206

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O06162 Citrate lyase subunit beta-like protein

Q5I0K3 Citrate lyase subunit beta-like protein, mitochondrial

Q8N0X4 Citrate lyase subunit beta-like protein, mitochondrial

Q8R4N0 Citrate lyase subunit beta-like protein, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005000	HpcH/HpaI aldolase
IPR015813	Pyruvate/Phosphoenolpyruvate kinase, catalytic core
IPR011206	Citrate lyase, beta subunit
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Schneider K, Dimroth P, Bott M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 9438-50 2000 [PubMed: 10924139] http://dx.doi.org/10.1021/bi000401r
2.	Morikawa J, Nishimura Y, Uchida A, Tanaka T. Molecular cloning of novel mouse and human putative citrate lyase beta-subunit. Biochem. Biophys. Res. Commun. 289 1282-6 2001 [PubMed: 11741334] http://dx.doi.org/10.1006/bbrc.2001.6125

Additional Reading Open in usermanual
	Goulding CW, Bowers PM, Segelke B, Lekin T, Kim CY, Terwilliger TC, Eisenberg D. The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function. J. Mol. Biol. 365 2007 275-83 [PubMed: 17064730] http://dx.doi.org/10.1016/j.jmb.2006.09.086

InterPro 23.1