Protein MalY - Escherichia coli (strain K12)

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P23256 (MALY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 112. 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:
Protein MalY

Including the following 2 domains:

Cystathionine beta-lyase MalY
Short name=CBL
EC=4.4.1.8
Alternative name(s):
Beta-cystathionase
Cysteine lyase
Maltose regulon modulator

Gene names

Name:	malY
Ordered Locus Names:	b1622, JW1614

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a beta-cystathionase and as a repressor of the maltose regulon.
Catalytic activity	L-cystathionine + H₂O = L-homocysteine + NH₃ + pyruvate. Ref.5
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Subunit structure	Homodimer. Interacts with MalT. Ref.6
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis Transcription Transcription regulation
Ligand	Pyridoxal phosphate
Molecular function	Lyase Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-cysteine desulfhydrase activity Inferred from mutant phenotype. Source: EcoCyc cystathionine beta-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 390

390

Protein MalY

PRO_0000163847

Amino acid modifications

Modified residue

233

N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis

233

K → I: Loss of enzymatic activity; but no loss of repression function. Ref.5

Secondary structure

390

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23256 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 7FAF15D76545DDB0
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FASTA

390

43,642

        10         20         30         40         50         60 
MFDFSKVVDR HGTWCTQWDY VADRFGTADL LPFTISDMDF ATAPCIIEAL NQRLMHGVFG 

        70         80         90        100        110        120 
YSRWKNDEFL AAIAHWFSTQ HYTAIDSQTV VYGPSVIYMV SELIRQWSET GEGVVIHTPA 

       130        140        150        160        170        180 
YDAFYKAIEG NQRTVMPVAL EKQADGWFCD MGKLEAVLAK PECKIMLLCS PQNPTGKVWT 

       190        200        210        220        230        240 
CDELEIMADL CERHGVRVIS DEIHMDMVWG EQPHIPWSNV ARGDWALLTS GSKSFNIPAL 

       250        260        270        280        290        300 
TGAYGIIENS SSRDAYLSAL KGRDGLSSPS VLALTAHIAA YQQGAPWLDA LRIYLKDNLT 

       310        320        330        340        350        360 
YIADKMNAAF PELNWQIPQS TYLAWLDLRP LNIDDNALQK ALIEQEKVAI MPGYTYGEEG 

       370        380        390 
RGFVRLNAGC PRSKLEKGVA GLINAIRAVR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system." Reidl J., Boos W. J. Bacteriol. 173:4862-4876(1991) [PubMed: 1856179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	"MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase)." Zdych E., Peist R., Reidl J., Boos W. J. Bacteriol. 177:5035-5039(1995) [PubMed: 7665481] [Abstract] Cited for: CATALYTIC ACTIVITY, PYRIDOXAL PHOSPHATE AT LYS-233, MUTAGENESIS OF LYS-233.
[6]	"X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression." Clausen T., Schlegel A., Peist R., Schneider E., Steegborn C., Chang Y.S., Haase A., Bourenkov G.P., Bartunik H.D., Boos W. EMBO J. 19:831-842(2000) [PubMed: 10698925] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF WILD TYPE AND MUTANT VAL-221 IN COMPLEX WITH WITH PYRIDOXAL PHOSPHATE, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-233.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M60722 mRNA. Translation: AAA24099.1.
U00096 Genomic DNA. Translation: AAC74694.1.
AP009048 Genomic DNA. Translation: BAA15373.1.

PIR

C42477.

RefSeq

NP_416139.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D2F	X-ray	2.50	A/B	1-390	[»]

ProteinModelPortal

P23256.

SMR

P23256. Positions 2-390.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10151N.

IntAct

P23256. 10 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000485; EBESCP00000000485; EBESCG00000000405.
EBESCT00000015523; EBESCP00000014814; EBESCG00000014583.

GeneID

945937.

GenomeReviews

Gene locus JW1614 in contig AP009048_GR.
Gene locus b1622 in contig U00096_GR.

KEGG

ecj:JW1614.
eco:b1622.

PATRIC

32118546. VBIEscCol129921_1693.

Organism-specific databases

EchoBASE

EB0559.

EcoGene

EG10564. malY.

Phylogenomic databases

eggNOG

COG1168.

GeneTree

EBGT00050000008899.

HOGENOM

HBG681988.

OMA

LVYGPSV.

PhylomeDB

P23256.

ProtClustDB

CLSK880149.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10564-MONOMER.
MetaCyc:EG10564-MONOMER.

Gene expression databases

Genevestigator

P23256.

Family and domain databases

InterPro

IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
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.

K14155.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00599. AA_TRANSFER_CLASS_2. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MALY_ECOLI

Accession

Primary (citable) accession number: P23256

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	January 25, 2012
This is version 112 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

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents