Cystathionine beta-lyase MetC - Escherichia coli (strain K12)

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P06721 (METC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cystathionine beta-lyase MetC
Short name=CBL
EC=4.4.1.8

Alternative name(s):
Beta-cystathionase
Cysteine lyase

Gene names

Name:	metC
Ordered Locus Names:	b3008, JW2975

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-cystathionine + H₂O = L-homocysteine + NH₃ + pyruvate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Subunit structure	Homotetramer. Ref.6
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the trans-sulfuration enzymes family.
Sequence caution	The sequence AAA69175.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-cysteine desulfhydrase activity Inferred from mutant phenotype PubMed 12883870. Source: EcoCyc cystathionine beta-lyase activity Inferred from direct assay Ref.1. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 395

395

Cystathionine beta-lyase MetC

PRO_0000114768

Amino acid modifications

Modified residue

210

N6-(pyridoxal phosphate)lysine

Secondary structure

395

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P06721 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: FD3308423D6427C6
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FASTA

395

43,212

        10         20         30         40         50         60 
MADKKLDTQL VNAGRSKKYT LGAVNSVIQR ASSLVFDSVE AKKHATRNRA NGELFYGRRG 

        70         80         90        100        110        120 
TLTHFSLQQA MCELEGGAGC VLFPCGAAAV ANSILAFIEQ GDHVLMTNTA YEPSQDFCSK 

       130        140        150        160        170        180 
ILSKLGVTTS WFDPLIGADI VKHLQPNTKI VFLESPGSIT MEVHDVPAIV AAVRSVVPDA 

       190        200        210        220        230        240 
IIMIDNTWAA GVLFKALDFG IDVSIQAATK YLVGHSDAMI GTAVCNARCW EQLRENAYLM 

       250        260        270        280        290        300 
GQMVDADTAY ITSRGLRTLG VRLRQHHESS LKVAEWLAEH PQVARVNHPA LPGSKGHEFW 

       310        320        330        340        350        360 
KRDFTGSSGL FSFVLKKKLN NEELANYLDN FSLFSMAYSW GGYESLILAN QPEHIAAIRP 

       370        380        390 
QGEIDFSGTL IRLHIGLEDV DDLIADLDAG FARIV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region." Belfaiza J., Parsot C., Martel A., de la Tour C.B., Margarita D., Cohen G.N., Saint-Girons I. Proc. Natl. Acad. Sci. U.S.A. 83:867-871(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences." Martel A., Bouthier de la Tour C., Le Goffic F. Biochem. Biophys. Res. Commun. 147:565-571(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 194-221.
[5]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[6]	"Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A." Clausen T., Huber R., Laber B., Pohlenz H.-D., Messerschmidt A. J. Mol. Biol. 262:202-224(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-210.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12858 Genomic DNA. Translation: AAA24158.1.
U28377 Genomic DNA. Translation: AAA69175.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76044.1.
AP009048 Genomic DNA. Translation: BAE77065.1.

PIR

WZECCB. A25153.

RefSeq

NP_417481.1. NC_000913.2.
YP_491201.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CL1	X-ray	1.83	A/B	1-395	[»]
1CL2	X-ray	2.20	A/B	1-395	[»]
2FQ6	X-ray	1.78	A/B	1-395	[»]
2GQN	X-ray	1.80	A/B	1-395	[»]

ProteinModelPortal

P06721.

SMR

P06721. Positions 4-395.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10193N.

IntAct

P06721. 6 interactions.

STRING

511145.b3008.

Proteomic databases

PaxDb

P06721.

PRIDE

P06721.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76044; AAC76044; b3008.
BAE77065; BAE77065; BAE77065.

GeneID

12932425.
946240.

KEGG

ecj:Y75_p2935.
eco:b3008.

PATRIC

32121430. VBIEscCol129921_3102.

Organism-specific databases

EchoBASE

EB0578.

EcoGene

EG10583. metC.

Phylogenomic databases

eggNOG

COG0626.

HOGENOM

HOG000246416.

K01760.

OMA

REQSYLM.

ProtClustDB

PRK08114.

Enzyme and pathway databases

BioCyc

EcoCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
ECOL316407:JW2975-MONOMER.
MetaCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.

UniPathway

UPA00051; UER00078.

Gene expression databases

Genevestigator

P06721.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR006233. Cys_b_lyase_bac.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

PANTHER

PTHR11808. PTHR11808. 1 hit.
PTHR11808:SF8. PTHR11808:SF8. 1 hit.

Pfam

PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]

PIRSF

PIRSF001434. CGS. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR01324. cysta_beta_ly_B. 1 hit.

PROSITE

PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075079.

EvolutionaryTrace

P06721.

Entry information

Entry name

METC_ECOLI

Accession

Primary (citable) accession number: P06721
Secondary accession number(s): Q2M9J1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents