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InterPro: IPR006233 Cystathionine beta-lyase, bacterial

Protein matches Help

UniProtKB

Matches:

581 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006233 Cys_b_lyase_bac

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR11808:SF8	Cys_b_lyase_bac	563
TIGRFAMs	TIGR01324	cysta_beta_ly_B	556
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000277 Cys/Met metabolism, pyridoxal phosphate-dependent enzyme

Contains

IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR015422 Pyridoxal phosphate-dependent transferase, major region, subdomain 2
IPR015424 Pyridoxal phosphate-dependent transferase, major domain

GO Term annotation Help

Process

GO:0006520 cellular amino acid metabolic process

Function

GO:0004121 cystathionine beta-lyase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

Cystathionine beta-lyase (alternate name: beta-cystathionase) is one of several pyridoxal-dependent enzymes of cysteine, methionine, and homocysteine metabolism. This enzyme is involved in the biosynthesis of Met from Cys [1].

Structural links Help

PDB - click here

SCOP: c.67.1.3

CATH: 3.40.640.10 , 3.90.1150.10

Database links Help

Enzyme: EC:4.4.1.8

CAZy: GH32

CluSTr: ALLvsALL:34096:77

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006233

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P06721 Cystathionine beta-lyase metC

P43623 Putative cystathionine beta-lyase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR015424	Pyridoxal phosphate-dependent transferase, major domain
IPR000277	Cys/Met metabolism, pyridoxal phosphate-dependent enzyme
IPR015422	Pyridoxal phosphate-dependent transferase, major region, subdomain 2
IPR015421	Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR006233	Cystathionine beta-lyase, bacterial
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. J. Mol. Biol. 262 202-24 1996 [PubMed: 8831789] http://dx.doi.org/10.1006/jmbi.1996.0508

Additional Reading Open in usermanual
	Clausen T, Huber R, Messerschmidt A, Pohlenz HD, Laber B. Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study. Biochemistry 36 1997 12633-43 [PubMed: 9376370] http://dx.doi.org/10.1021/bi970630m
	Ejim LJ, Blanchard JE, Koteva KP, Sumerfield R, Elowe NH, Chechetto JD, Brown ED, Junop MS, Wright GD. Inhibitors of bacterial cystathionine beta-lyase: leads for new antimicrobial agents and probes of enzyme structure and function. J. Med. Chem. 50 2007 755-64 [PubMed: 17300162] http://dx.doi.org/10.1021/jm061132r

InterPro 24.0