MALY_ECOLI
ID MALY_ECOLI Reviewed; 390 AA.
AC P23256;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein MalY;
DE Includes:
DE RecName: Full=Cystathionine beta-lyase MalY;
DE Short=CBL;
DE EC=4.4.1.13 {ECO:0000269|PubMed:7665481};
DE AltName: Full=Beta-cystathionase MalY;
DE AltName: Full=Cysteine lyase MalY;
DE AltName: Full=Cysteine-S-conjugate beta-lyase MalY;
DE Includes:
DE RecName: Full=Maltose regulon modulator;
GN Name=malY; OrderedLocusNames=b1622, JW1614;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1856179; DOI=10.1128/jb.173.15.4862-4876.1991;
RA Reidl J., Boos W.;
RT "The malX malY operon of Escherichia coli encodes a novel enzyme II of the
RT phosphotransferase system recognizing glucose and maltose and an enzyme
RT abolishing the endogenous induction of the maltose system.";
RL J. Bacteriol. 173:4862-4876(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CATALYTIC ACTIVITY, PYRIDOXAL PHOSPHATE AT LYS-233, AND MUTAGENESIS OF
RP LYS-233.
RX PubMed=7665481; DOI=10.1128/jb.177.17.5035-5039.1995;
RA Zdych E., Peist R., Reidl J., Boos W.;
RT "MalY of Escherichia coli is an enzyme with the activity of a beta C-S
RT lyase (cystathionase).";
RL J. Bacteriol. 177:5035-5039(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF WILD TYPE AND MUTANT VAL-221 IN
RP COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT, AND PYRIDOXAL PHOSPHATE AT
RP LYS-233.
RX PubMed=10698925; DOI=10.1093/emboj/19.5.831;
RA Clausen T., Schlegel A., Peist R., Schneider E., Steegborn C., Chang Y.S.,
RA Haase A., Bourenkov G.P., Bartunik H.D., Boos W.;
RT "X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-
RT dependent enzyme acting as a modulator in mal gene expression.";
RL EMBO J. 19:831-842(2000).
CC -!- FUNCTION: Acts as a beta-cystathionase and as a repressor of the
CC maltose regulon.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000269|PubMed:7665481};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC Evidence={ECO:0000269|PubMed:7665481};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10698925, ECO:0000269|PubMed:7665481};
CC -!- SUBUNIT: Homodimer. Interacts with MalT. {ECO:0000269|PubMed:10698925}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000305}.
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DR EMBL; M60722; AAA24099.1; -; mRNA.
DR EMBL; U00096; AAC74694.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15373.1; -; Genomic_DNA.
DR PIR; C42477; C42477.
DR RefSeq; NP_416139.1; NC_000913.3.
DR RefSeq; WP_000459379.1; NZ_SSZK01000001.1.
DR PDB; 1D2F; X-ray; 2.50 A; A/B=1-390.
DR PDBsum; 1D2F; -.
DR AlphaFoldDB; P23256; -.
DR SMR; P23256; -.
DR BioGRID; 4261731; 9.
DR DIP; DIP-10151N; -.
DR IntAct; P23256; 10.
DR STRING; 511145.b1622; -.
DR MoonProt; P23256; -.
DR jPOST; P23256; -.
DR PaxDb; P23256; -.
DR PRIDE; P23256; -.
DR EnsemblBacteria; AAC74694; AAC74694; b1622.
DR EnsemblBacteria; BAA15373; BAA15373; BAA15373.
DR GeneID; 945937; -.
DR KEGG; ecj:JW1614; -.
DR KEGG; eco:b1622; -.
DR PATRIC; fig|1411691.4.peg.639; -.
DR EchoBASE; EB0559; -.
DR eggNOG; COG1168; Bacteria.
DR HOGENOM; CLU_017584_15_0_6; -.
DR InParanoid; P23256; -.
DR OMA; RINIGCP; -.
DR PhylomeDB; P23256; -.
DR BioCyc; EcoCyc:EG10564-MON; -.
DR BioCyc; MetaCyc:EG10564-MON; -.
DR SABIO-RK; P23256; -.
DR EvolutionaryTrace; P23256; -.
DR PRO; PR:P23256; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IDA:EcoCyc.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:EcoCyc.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR027619; C_S_lyase_PatB.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR04350; C_S_lyase_PatB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Lyase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..390
FT /note="Protein MalY"
FT /id="PRO_0000163847"
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:10698925,
FT ECO:0000269|PubMed:7665481"
FT MUTAGEN 233
FT /note="K->I: Loss of enzymatic activity; but no loss of
FT repression function."
FT /evidence="ECO:0000269|PubMed:7665481"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:1D2F"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1D2F"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 285..309
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:1D2F"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:1D2F"
FT HELIX 372..389
FT /evidence="ECO:0007829|PDB:1D2F"
SQ SEQUENCE 390 AA; 43642 MW; 7FAF15D76545DDB0 CRC64;
MFDFSKVVDR HGTWCTQWDY VADRFGTADL LPFTISDMDF ATAPCIIEAL NQRLMHGVFG
YSRWKNDEFL AAIAHWFSTQ HYTAIDSQTV VYGPSVIYMV SELIRQWSET GEGVVIHTPA
YDAFYKAIEG NQRTVMPVAL EKQADGWFCD MGKLEAVLAK PECKIMLLCS PQNPTGKVWT
CDELEIMADL CERHGVRVIS DEIHMDMVWG EQPHIPWSNV ARGDWALLTS GSKSFNIPAL
TGAYGIIENS SSRDAYLSAL KGRDGLSSPS VLALTAHIAA YQQGAPWLDA LRIYLKDNLT
YIADKMNAAF PELNWQIPQS TYLAWLDLRP LNIDDNALQK ALIEQEKVAI MPGYTYGEEG
RGFVRLNAGC PRSKLEKGVA GLINAIRAVR
