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Protein

Cystathionine beta-lyase MetC

Gene

metC

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

Functioni

Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis (PubMed:7049234). Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine (PubMed:12883870). In addition, under certain growth conditions, exhibits significant alanine racemase coactivity (PubMed:21193606).3 Publications

Catalytic activityi

L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate.1 Publication
L-cysteine + H2O = sulfide + NH3 + pyruvate.1 Publication

Cofactori

pyridoxal 5'-phosphate3 Publications

Enzyme regulationi

L-cysteine inhibits cystathionine beta-lyase activity competitively (PubMed:7049234). Inhibited by aminoethoxyvinylglycine (AVG) (PubMed:9376370).2 Publications

Kineticsi

  1. KM=0.04 mM for L-cystathionine1 Publication
  2. KM=0.25 mM for L-cystine1 Publication
  1. Vmax=249 µmol/min/mg enzyme with L-cystathionine as substrate1 Publication
  2. Vmax=263 µmol/min/mg enzyme with L-cystine as substrate1 Publication

pH dependencei

Optimum pH is 8.0-9.0.1 Publication

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from L-cystathionine.Curated
Proteins known to be involved in this subpathway in this organism are:
  1. Cystathionine beta-lyase MetC (metC)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homocysteine from L-cystathionine, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

GO - Molecular functioni

  • cystathionine beta-lyase activity Source: EcoCyc
  • L-cysteine desulfhydrase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:CYSTATHIONINE-BETA-LYASE-MONOMER
MetaCyc:CYSTATHIONINE-BETA-LYASE-MONOMER
BRENDAi4.4.1.8 2026
UniPathwayiUPA00051; UER00078

Names & Taxonomyi

Protein namesi
Recommended name:
Cystathionine beta-lyase MetC1 Publication (EC:4.4.1.81 Publication)
Short name:
CBL1 Publication
Short name:
CL1 Publication
Alternative name(s):
Beta-cystathionase1 Publication
Cysteine desulfhydrase1 Publication (EC:4.4.1.281 Publication)
Short name:
CD1 Publication
Cysteine lyase
Gene namesi
Name:metC1 Publication
Ordered Locus Names:b3008, JW2975
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10583 metC

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Disruption of the gene increases the amounts of L-cysteine and L-cystine produced after 72 hours of cultivation.1 Publication

Chemistry databases

ChEMBLiCHEMBL1075079

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001147682 – 395Cystathionine beta-lyase MetCAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei210N6-(pyridoxal phosphate)lysine2 Publications1

Proteomic databases

PaxDbiP06721
PRIDEiP06721

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.1 Publication

Protein-protein interaction databases

BioGridi4261419, 41 interactors
DIPiDIP-10193N
IntActiP06721, 6 interactors
STRINGi316385.ECDH10B_3183

Chemistry databases

BindingDBiP06721

Structurei

Secondary structure

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 12Combined sources7
Helixi17 – 20Combined sources4
Beta strandi23 – 25Combined sources3
Beta strandi32 – 34Combined sources3
Helixi39 – 47Combined sources9
Turni48 – 52Combined sources5
Helixi57 – 59Combined sources3
Helixi62 – 75Combined sources14
Beta strandi78 – 85Combined sources8
Helixi86 – 97Combined sources12
Beta strandi103 – 107Combined sources5
Helixi112 – 120Combined sources9
Helixi122 – 125Combined sources4
Beta strandi128 – 132Combined sources5
Helixi137 – 143Combined sources7
Beta strandi148 – 156Combined sources9
Turni158 – 160Combined sources3
Helixi166 – 176Combined sources11
Beta strandi181 – 185Combined sources5
Turni187 – 192Combined sources6
Helixi196 – 199Combined sources4
Beta strandi202 – 207Combined sources6
Turni208 – 213Combined sources6
Beta strandi215 – 217Combined sources3
Beta strandi221 – 225Combined sources5
Turni227 – 229Combined sources3
Helixi230 – 239Combined sources10
Helixi246 – 256Combined sources11
Helixi259 – 278Combined sources20
Beta strandi283 – 287Combined sources5
Helixi297 – 303Combined sources7
Beta strandi309 – 317Combined sources9
Helixi321 – 328Combined sources8
Beta strandi342 – 344Combined sources3
Beta strandi346 – 350Combined sources5
Helixi352 – 356Combined sources5
Beta strandi370 – 374Combined sources5
Helixi380 – 392Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CL1X-ray1.83A/B1-395[»]
1CL2X-ray2.20A/B1-395[»]
2FQ6X-ray1.78A/B1-395[»]
2GQNX-ray1.80A/B1-395[»]
4ITGX-ray1.74A/B1-395[»]
4ITXX-ray1.61A/B1-395[»]
ProteinModelPortaliP06721
SMRiP06721
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06721

Family & Domainsi

Sequence similaritiesi

Belongs to the trans-sulfuration enzymes family.Curated

Phylogenomic databases

eggNOGiENOG4105C28 Bacteria
COG0626 LUCA
HOGENOMiHOG000246416
InParanoidiP06721
KOiK01760
OMAiPTHFAFQ
PhylomeDBiP06721

Family and domain databases

CDDicd00614 CGS_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
InterProiView protein in InterPro
IPR000277 Cys/Met-Metab_PyrdxlP-dep_enz
IPR006233 Cys_b_lyase_bac
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR43500 PTHR43500, 1 hit
PfamiView protein in Pfam
PF01053 Cys_Met_Meta_PP, 1 hit
PIRSFiPIRSF001434 CGS, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01324 cysta_beta_ly_B, 1 hit
PROSITEiView protein in PROSITE
PS00868 CYS_MET_METAB_PP, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_001301079.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76044; AAC76044; b3008
BAE77065; BAE77065; BAE77065
GeneIDi946240
KEGGiecj:JW2975
eco:b3008
PATRICifig|511145.12.peg.3102

Similar proteinsi

Entry informationi

Entry nameiMETC_ECOLI
AccessioniPrimary (citable) accession number: P06721
Secondary accession number(s): Q2M9J1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: March 28, 2018
This is version 159 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health