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MHPD_ECOLI
ID   MHPD_ECOLI              Reviewed;         269 AA.
AC   P77608; P71205; P77045; Q2MC74;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=2-keto-4-pentenoate hydratase;
DE            EC=4.2.1.80 {ECO:0000269|PubMed:9492273};
DE   AltName: Full=2-hydroxypentadienoic acid hydratase {ECO:0000303|PubMed:9492273};
GN   Name=mhpD {ECO:0000303|PubMed:9492273}; OrderedLocusNames=b0350, JW0341;
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 / W3110 / ATCC 27325 / DSM 5911;
RA   Kawamukai M.;
RT   "Complete sequence of the mhp operon.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / CS520;
RX   PubMed=9098055; DOI=10.1128/jb.179.8.2573-2581.1997;
RA   Ferrandez A., Garcia J.L., Diaz E.;
RT   "Genetic characterization and expression in heterologous hosts of the 3-(3-
RT   hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12.";
RL   J. Bacteriol. 179:2573-2581(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
RP   PROTEIN SEQUENCE OF 1-6, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9492273; DOI=10.1046/j.1432-1327.1998.2510098.x;
RA   Pollard J.R., Bugg T.D.H.;
RT   "Purification, characterisation and reaction mechanism of monofunctional 2-
RT   hydroxypentadienoic acid hydratase from Escherichia coli.";
RL   Eur. J. Biochem. 251:98-106(1998).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RG   New York structural genomix research consortium (NYSGXRC);
RT   "Crystal structure of 2-hydroxypentadienoic acid hydratase from Escherichia
RT   coli.";
RL   Submitted (JAN-2005) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the conversion of 2-hydroxypentadienoic acid
CC       (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid.
CC       {ECO:0000269|PubMed:9492273}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-hydroxy-2-oxopentanoate = (2Z)-2-hydroxypenta-2,4-
CC         dienoate + H2O; Xref=Rhea:RHEA:22580, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:67152, ChEBI:CHEBI:73143; EC=4.2.1.80;
CC         Evidence={ECO:0000269|PubMed:9492273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:9492273};
CC       Note=Divalent metal ions. Optimum activity is obtained with Mn(2+).
CC       {ECO:0000269|PubMed:9492273};
CC   -!- ACTIVITY REGULATION: Inhibited by sodium oxalate.
CC       {ECO:0000269|PubMed:9492273}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=41 uM for 2-hydroxy-pentadienoic acid (at pH 6)
CC         {ECO:0000269|PubMed:9492273};
CC         Note=kcat is 450 sec(-1). {ECO:0000269|PubMed:9492273};
CC       pH dependence:
CC         Optimum pH is 5.5-8.0, but decreases linearly above pH 8.3, and shows
CC         an inflection at pH 5.5. {ECO:0000269|PubMed:9492273};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC       {ECO:0000305|PubMed:9492273}.
CC   -!- SIMILARITY: Belongs to the hydratase/decarboxylase family. MhpD
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB18074.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA13055.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D86239; BAA13055.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Y09555; CAA70750.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18074.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73453.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76132.1; -; Genomic_DNA.
DR   PIR; F64762; F64762.
DR   RefSeq; NP_414884.2; NC_000913.3.
DR   RefSeq; WP_000160710.1; NZ_SSZK01000061.1.
DR   PDB; 1SV6; X-ray; 2.90 A; A/B/C/D/E=1-269.
DR   PDB; 2WQT; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-269.
DR   PDBsum; 1SV6; -.
DR   PDBsum; 2WQT; -.
DR   AlphaFoldDB; P77608; -.
DR   SMR; P77608; -.
DR   BioGRID; 4260731; 5.
DR   IntAct; P77608; 3.
DR   STRING; 511145.b0350; -.
DR   SwissLipids; SLP:000001886; -.
DR   jPOST; P77608; -.
DR   PaxDb; P77608; -.
DR   PRIDE; P77608; -.
DR   EnsemblBacteria; AAC73453; AAC73453; b0350.
DR   EnsemblBacteria; BAE76132; BAE76132; BAE76132.
DR   GeneID; 944768; -.
DR   KEGG; ecj:JW0341; -.
DR   KEGG; eco:b0350; -.
DR   PATRIC; fig|1411691.4.peg.1928; -.
DR   EchoBASE; EB4022; -.
DR   eggNOG; COG3971; Bacteria.
DR   HOGENOM; CLU_060136_4_1_6; -.
DR   InParanoid; P77608; -.
DR   OMA; IRDWSIG; -.
DR   PhylomeDB; P77608; -.
DR   BioCyc; EcoCyc:MHPDHYDROL-MON; -.
DR   BioCyc; MetaCyc:MHPDHYDROL-MON; -.
DR   BRENDA; 4.2.1.80; 2165.
DR   SABIO-RK; P77608; -.
DR   UniPathway; UPA00714; -.
DR   EvolutionaryTrace; P77608; -.
DR   PRO; PR:P77608; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0008684; F:2-oxopent-4-enoate hydratase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019439; P:aromatic compound catabolic process; NAS:EcoliWiki.
DR   Gene3D; 3.90.850.10; -; 1.
DR   HAMAP; MF_01655; MhpD; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR023793; Keto_pentenoate-hydratase.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW   Lyase; Reference proteome.
FT   CHAIN           1..269
FT                   /note="2-keto-4-pentenoate hydratase"
FT                   /id="PRO_0000096469"
FT   CONFLICT        202
FT                   /note="G -> E (in Ref. 1; BAA13055)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..19
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           27..30
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           35..51
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           66..70
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          103..114
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           123..127
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          130..140
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           151..156
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          163..166
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          190..196
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   HELIX           204..217
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          227..234
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          244..249
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:2WQT"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:2WQT"
SQ   SEQUENCE   269 AA;  28890 MW;  34A81A8A4E236358 CRC64;
     MTKHTLEQLA ADLRRAAEQG EAIAPLRDLI GIDNAEAAYA IQHINVQHDV AQGRRVVGRK
     VGLTHPKVQQ QLGVDQPDFG TLFADMCYGD NEIIPFSRVL QPRIEAEIAL VLNRDLPATD
     ITFDELYNAI EWVLPALEVV GSRIRDWSIQ FVDTVADNAS CGVYVIGGPA QRPAGLDLKN
     CAMKMTRNNE EVSSGRGSEC LGHPLNAAVW LARKMASLGE PLRTGDIILT GALGPMVAVN
     AGDRFEAHIE GIGSVAATFS SAAPKGSLS
 
 
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