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P06721

- METC_ECOLI

UniProt

P06721 - METC_ECOLI

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Protein

Cystathionine beta-lyase MetC

Gene

metC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate.

Cofactori

Pyridoxal phosphate.

Pathwayi

GO - Molecular functioni

  1. cystathionine beta-lyase activity Source: EcoCyc
  2. L-cysteine desulfhydrase activity Source: EcoCyc
  3. pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  1. methionine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
ECOL316407:JW2975-MONOMER.
MetaCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
UniPathwayiUPA00051; UER00078.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine beta-lyase MetC (EC:4.4.1.8)
Short name:
CBL
Alternative name(s):
Beta-cystathionase
Cysteine lyase
Gene namesi
Name:metC
Ordered Locus Names:b3008, JW2975
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10583. metC.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Cystathionine beta-lyase MetCPRO_0000114768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP06721.
PRIDEiP06721.

Expressioni

Gene expression databases

GenevestigatoriP06721.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-10193N.
IntActiP06721. 6 interactions.
STRINGi511145.b3008.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127
Helixi17 – 204
Beta strandi23 – 253
Helixi39 – 479
Turni48 – 525
Turni57 – 593
Helixi62 – 7514
Beta strandi78 – 858
Helixi86 – 9510
Beta strandi103 – 1075
Helixi112 – 1209
Helixi122 – 1254
Beta strandi128 – 1325
Helixi137 – 1437
Beta strandi148 – 1569
Turni158 – 1603
Helixi166 – 17611
Beta strandi181 – 1855
Turni187 – 1926
Helixi196 – 1994
Beta strandi202 – 2076
Turni208 – 2136
Beta strandi215 – 2173
Beta strandi221 – 2255
Turni227 – 2293
Helixi230 – 23910
Helixi246 – 27833
Beta strandi283 – 2875
Helixi297 – 3037
Beta strandi309 – 3179
Helixi321 – 3288
Beta strandi342 – 3443
Beta strandi346 – 3505
Helixi352 – 3565
Beta strandi370 – 3745
Helixi380 – 39213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CL1X-ray1.83A/B1-395[»]
1CL2X-ray2.20A/B1-395[»]
2FQ6X-ray1.78A/B1-395[»]
2GQNX-ray1.80A/B1-395[»]
ProteinModelPortaliP06721.
SMRiP06721. Positions 4-395.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06721.

Family & Domainsi

Sequence similaritiesi

Belongs to the trans-sulfuration enzymes family.Curated

Phylogenomic databases

eggNOGiCOG0626.
HOGENOMiHOG000246416.
InParanoidiP06721.
KOiK01760.
OMAiEQSYLMG.
OrthoDBiEOG67DPN3.
PhylomeDBiP06721.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000277. 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]
PANTHERiPTHR11808. PTHR11808. 1 hit.
PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFiPIRSF001434. CGS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01324. cysta_beta_ly_B. 1 hit.
PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06721-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADKKLDTQL VNAGRSKKYT LGAVNSVIQR ASSLVFDSVE AKKHATRNRA
60 70 80 90 100
NGELFYGRRG TLTHFSLQQA MCELEGGAGC VLFPCGAAAV ANSILAFIEQ
110 120 130 140 150
GDHVLMTNTA YEPSQDFCSK ILSKLGVTTS WFDPLIGADI VKHLQPNTKI
160 170 180 190 200
VFLESPGSIT MEVHDVPAIV AAVRSVVPDA IIMIDNTWAA GVLFKALDFG
210 220 230 240 250
IDVSIQAATK YLVGHSDAMI GTAVCNARCW EQLRENAYLM GQMVDADTAY
260 270 280 290 300
ITSRGLRTLG VRLRQHHESS LKVAEWLAEH PQVARVNHPA LPGSKGHEFW
310 320 330 340 350
KRDFTGSSGL FSFVLKKKLN NEELANYLDN FSLFSMAYSW GGYESLILAN
360 370 380 390
QPEHIAAIRP QGEIDFSGTL IRLHIGLEDV DDLIADLDAG FARIV
Length:395
Mass (Da):43,212
Last modified:January 1, 1988 - v1
Checksum:iFD3308423D6427C6
GO

Sequence cautioni

The sequence AAA69175.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA25153. WZECCB.
RefSeqiNP_417481.1. NC_000913.3.
YP_491201.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76044; AAC76044; b3008.
BAE77065; BAE77065; BAE77065.
GeneIDi12932425.
946240.
KEGGiecj:Y75_p2935.
eco:b3008.
PATRICi32121430. VBIEscCol129921_3102.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A25153. WZECCB.
RefSeqi NP_417481.1. NC_000913.3.
YP_491201.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P06721.
SMRi P06721. Positions 4-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10193N.
IntActi P06721. 6 interactions.
STRINGi 511145.b3008.

Chemistry

ChEMBLi CHEMBL1075079.

Proteomic databases

PaxDbi P06721.
PRIDEi P06721.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76044 ; AAC76044 ; b3008 .
BAE77065 ; BAE77065 ; BAE77065 .
GeneIDi 12932425.
946240.
KEGGi ecj:Y75_p2935.
eco:b3008.
PATRICi 32121430. VBIEscCol129921_3102.

Organism-specific databases

EchoBASEi EB0578.
EcoGenei EG10583. metC.

Phylogenomic databases

eggNOGi COG0626.
HOGENOMi HOG000246416.
InParanoidi P06721.
KOi K01760.
OMAi EQSYLMG.
OrthoDBi EOG67DPN3.
PhylomeDBi P06721.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00078 .
BioCyci EcoCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
ECOL316407:JW2975-MONOMER.
MetaCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.

Miscellaneous databases

EvolutionaryTracei P06721.
PROi P06721.

Gene expression databases

Genevestigatori P06721.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11808. PTHR11808. 1 hit.
Pfami PF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view ]
PIRSFi PIRSF001434. CGS. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01324. cysta_beta_ly_B. 1 hit.
PROSITEi PS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiMETC_ECOLI
AccessioniPrimary (citable) accession number: P06721
Secondary accession number(s): Q2M9J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3