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Protein

Protein MalY

Gene

malY

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

Functioni

Acts as a beta-cystathionase and as a repressor of the maltose regulon.

Catalytic activityi

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

Cofactori

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Repressor

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis, Transcription, Transcription regulation

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:EG10564-MONOMER.
ECOL316407:JW1614-MONOMER.
MetaCyc:EG10564-MONOMER.
SABIO-RKP23256.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein MalY
Including the following 2 domains:
Cystathionine beta-lyase MalY (EC:4.4.1.8)
Short name:
CBL
Alternative name(s):
Beta-cystathionase
Cysteine lyase
Maltose regulon modulator
Gene namesi
Name:malY
Ordered Locus Names:b1622, JW1614
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10564. malY.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi233 – 2331K → I: Loss of enzymatic activity; but no loss of repression function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Protein MalYPRO_0000163847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP23256.
PRIDEiP23256.

Interactioni

Subunit structurei

Homodimer. Interacts with MalT.1 Publication

Protein-protein interaction databases

BioGridi4261731. 9 interactions.
DIPiDIP-10151N.
IntActiP23256. 10 interactions.
STRINGi511145.b1622.

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 373Combined sources
Helixi44 – 5411Combined sources
Helixi67 – 8014Combined sources
Helixi87 – 893Combined sources
Beta strandi90 – 945Combined sources
Helixi96 – 10611Combined sources
Beta strandi113 – 1197Combined sources
Helixi122 – 1309Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi144 – 1485Combined sources
Helixi151 – 1588Combined sources
Beta strandi163 – 1719Combined sources
Turni173 – 1753Combined sources
Helixi183 – 19311Combined sources
Beta strandi197 – 2015Combined sources
Turni203 – 2064Combined sources
Beta strandi210 – 2123Combined sources
Helixi217 – 2193Combined sources
Beta strandi223 – 2297Combined sources
Helixi232 – 2354Combined sources
Helixi238 – 2403Combined sources
Beta strandi243 – 2475Combined sources
Helixi250 – 26112Combined sources
Helixi271 – 28313Combined sources
Helixi285 – 30925Combined sources
Beta strandi322 – 3276Combined sources
Helixi329 – 3313Combined sources
Helixi335 – 34410Combined sources
Helixi353 – 3564Combined sources
Helixi358 – 3603Combined sources
Beta strandi363 – 3675Combined sources
Helixi372 – 38918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2FX-ray2.50A/B1-390[»]
ProteinModelPortaliP23256.
SMRiP23256. Positions 2-390.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23256.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C87. Bacteria.
COG1168. LUCA.
HOGENOMiHOG000223048.
InParanoidiP23256.
KOiK14155.
OMAiYCTQWDY.
PhylomeDBiP23256.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR027619. C_S_lyase_PatB.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR04350. C_S_lyase_PatB. 1 hit.

Sequencei

Sequence statusi: Complete.

P23256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDFSKVVDR HGTWCTQWDY VADRFGTADL LPFTISDMDF ATAPCIIEAL
60 70 80 90 100
NQRLMHGVFG YSRWKNDEFL AAIAHWFSTQ HYTAIDSQTV VYGPSVIYMV
110 120 130 140 150
SELIRQWSET GEGVVIHTPA YDAFYKAIEG NQRTVMPVAL EKQADGWFCD
160 170 180 190 200
MGKLEAVLAK PECKIMLLCS PQNPTGKVWT CDELEIMADL CERHGVRVIS
210 220 230 240 250
DEIHMDMVWG EQPHIPWSNV ARGDWALLTS GSKSFNIPAL TGAYGIIENS
260 270 280 290 300
SSRDAYLSAL KGRDGLSSPS VLALTAHIAA YQQGAPWLDA LRIYLKDNLT
310 320 330 340 350
YIADKMNAAF PELNWQIPQS TYLAWLDLRP LNIDDNALQK ALIEQEKVAI
360 370 380 390
MPGYTYGEEG RGFVRLNAGC PRSKLEKGVA GLINAIRAVR
Length:390
Mass (Da):43,642
Last modified:November 1, 1991 - v1
Checksum:i7FAF15D76545DDB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60722 mRNA. Translation: AAA24099.1.
U00096 Genomic DNA. Translation: AAC74694.1.
AP009048 Genomic DNA. Translation: BAA15373.1.
PIRiC42477.
RefSeqiNP_416139.1. NC_000913.3.
WP_000459379.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74694; AAC74694; b1622.
BAA15373; BAA15373; BAA15373.
GeneIDi945937.
KEGGiecj:JW1614.
eco:b1622.
PATRICi32118546. VBIEscCol129921_1693.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60722 mRNA. Translation: AAA24099.1.
U00096 Genomic DNA. Translation: AAC74694.1.
AP009048 Genomic DNA. Translation: BAA15373.1.
PIRiC42477.
RefSeqiNP_416139.1. NC_000913.3.
WP_000459379.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2FX-ray2.50A/B1-390[»]
ProteinModelPortaliP23256.
SMRiP23256. Positions 2-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261731. 9 interactions.
DIPiDIP-10151N.
IntActiP23256. 10 interactions.
STRINGi511145.b1622.

Proteomic databases

PaxDbiP23256.
PRIDEiP23256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74694; AAC74694; b1622.
BAA15373; BAA15373; BAA15373.
GeneIDi945937.
KEGGiecj:JW1614.
eco:b1622.
PATRICi32118546. VBIEscCol129921_1693.

Organism-specific databases

EchoBASEiEB0559.
EcoGeneiEG10564. malY.

Phylogenomic databases

eggNOGiENOG4105C87. Bacteria.
COG1168. LUCA.
HOGENOMiHOG000223048.
InParanoidiP23256.
KOiK14155.
OMAiYCTQWDY.
PhylomeDBiP23256.

Enzyme and pathway databases

BioCyciEcoCyc:EG10564-MONOMER.
ECOL316407:JW1614-MONOMER.
MetaCyc:EG10564-MONOMER.
SABIO-RKP23256.

Miscellaneous databases

EvolutionaryTraceiP23256.
PROiP23256.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR027619. C_S_lyase_PatB.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR04350. C_S_lyase_PatB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMALY_ECOLI
AccessioniPrimary (citable) accession number: P23256
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 7, 2016
This is version 144 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, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.