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

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P06721 (METC_ECOLI)

Last modified November 3, 2009. Version 96. History...

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

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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.5
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the trans-sulfuration enzymes family.

Hide | Top

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
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	cystathionine beta-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

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...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P06721-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: FD3308423D6427C6
Show »

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

Hide | Top

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: 3513164] [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: 9278503] [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: 16738553] [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: 3307782] [Abstract] Cited for: PROTEIN SEQUENCE OF 194-221.
[5]	"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: 8831789] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-210.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

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

AP_003559.1.
NP_417481.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10193N.

STRING

P06721.

2-D gel databases

ECO2DBASE

G043.0. 6TH EDITION.

Proteomic databases

PRIDE

P06721.

Genome annotation databases

GeneID

946240.

GenomeReviews

Gene locus JW2975 in contig AP009048_GR.
Gene locus b3008 in contig U00096_GR.

KEGG

ecj:JW2975.
eco:b3008.

Organism-specific databases

EchoBASE

EB0578.

EcoGene

EG10583. metC.

CMR

Search...

Phylogenomic databases

HOGENOM

P06721.

OMA

IETTYYD.

Enzyme and pathway databases

BioCyc

EcoCyc:CYSTATHIONINE-BETA-LYASE-MON.
MetaCyc:CYSTATHIONINE-BETA-LYASE-MON.

Gene expression databases

Genevestigator

P06721.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

PANTHER

PTHR11808:SF8. Cys_b_lyase_bac. 1 hit.
PTHR11808. Cys_Met_Meta_PP. 1 hit.

Pfam

PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]

PIRSF

PIRSF001434. CGS. 1 hit.

TIGRFAMs

TIGR01324. cysta_beta_ly_B. 1 hit.

PROSITE

PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

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:	November 3, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top