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KATG_ECOLI
ID   KATG_ECOLI              Reviewed;         726 AA.
AC   P13029; Q2M8N8;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Hydroperoxidase I {ECO:0000303|PubMed:374409};
DE            Short=HPI {ECO:0000303|PubMed:374409};
DE   AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
GN   OrderedLocusNames=b3942, JW3914;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3045098; DOI=10.1128/jb.170.9.4415-4419.1988;
RA   Triggs-Raine B.L., Doble B.W., Mulvey M.R., Sorby P.A., Loewen P.C.;
RT   "Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli.";
RL   J. Bacteriol. 170:4415-4419(1988).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-339.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 309-726.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT   from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [6]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, HEME-BINDING, AND
RP   COFACTOR.
RX   PubMed=374409; DOI=10.1016/s0021-9258(18)50722-5;
RA   Claiborne A., Fridovich I.;
RT   "Purification of the o-dianisidine peroxidase from Escherichia coli B.";
RL   J. Biol. Chem. 254:4245-4252(1979).
RN   [7]
RP   COVALENT BOND.
RX   PubMed=12832453; DOI=10.1074/jbc.m304053200;
RA   Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T.,
RA   Singh R., Switala J., Carpena X., Fita I., Loewen P.C.;
RT   "Characterization of the catalase-peroxidase KatG from Burkholderia
RT   pseudomallei by mass spectrometry.";
RL   J. Biol. Chem. 278:35687-35692(2003).
RN   [8]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
RA   Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
RT   "Comparative study of catalase-peroxidases (KatGs).";
RL   Arch. Biochem. Biophys. 471:207-214(2008).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=23416055; DOI=10.1016/j.celrep.2013.01.026;
RA   Dorsey-Oresto A., Lu T., Mosel M., Wang X., Salz T., Drlica K., Zhao X.;
RT   "YihE kinase is a central regulator of programmed cell death in bacteria.";
RL   Cell Rep. 3:528-537(2013).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 422-726.
RX   PubMed=15388929; DOI=10.1107/s0907444904020621;
RA   Carpena X., Melik-Adamyan W., Loewen P.C., Fita I.;
RT   "Structure of the C-terminal domain of the catalase-peroxidase KatG from
RT   Escherichia coli.";
RL   Acta Crystallogr. D 60:1824-1832(2004).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. Also displays NADH oxidase, INH lyase and
CC       isonicotinoyl-NAD synthase activities. {ECO:0000269|PubMed:18178143,
CC       ECO:0000269|PubMed:23416055, ECO:0000269|PubMed:374409}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:374409};
CC       Note=Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.
CC       {ECO:0000269|PubMed:374409};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=35 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
CC         {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC         KM=4.2 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC         {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC         KM=3.9 mM for H(2)O(2) for the catalase reaction (at pH 7.5)
CC         {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC         KM=60 uM for H(2)O(2) for the peroxidase reaction
CC         {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC         KM=24 uM for ABTS for the peroxidase reaction
CC         {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC         Vmax=3730 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC         (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143,
CC         ECO:0000269|PubMed:374409};
CC         Vmax=2220 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC         (at pH 7.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC         Vmax=18 umol/min/mg enzyme for ABTS for the peroxidase reaction
CC         {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC       pH dependence:
CC         Optimum pH is 4.25 for the peroxidase reaction and 7.5 for the
CC         catalase reaction. {ECO:0000269|PubMed:18178143,
CC         ECO:0000269|PubMed:374409};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:374409}.
CC   -!- INDUCTION: By hydrogen peroxide.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC       for the catalase, but not the peroxidase activity of the enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- DISRUPTION PHENOTYPE: Cells are more sensitive to killing by nalidixic
CC       acid, the effect is mitigated by pretreatment with 2,2'-bipyridyl and
CC       thiourea, both of which inhibit hydroxyl radical accumulation.
CC       {ECO:0000269|PubMed:23416055}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR   EMBL; M21516; AAA24040.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76924.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77368.1; -; Genomic_DNA.
DR   EMBL; L19201; AAB03074.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43048.1; -; Genomic_DNA.
DR   PIR; A65201; CSECHP.
DR   RefSeq; NP_418377.1; NC_000913.3.
DR   RefSeq; WP_001295695.1; NZ_SSZK01000014.1.
DR   PDB; 1U2J; X-ray; 2.30 A; A/B/C/D/E/F/G/H=422-726.
DR   PDB; 1U2K; X-ray; 2.00 A; A=422-726.
DR   PDB; 1U2L; X-ray; 2.30 A; A/B=422-726.
DR   PDBsum; 1U2J; -.
DR   PDBsum; 1U2K; -.
DR   PDBsum; 1U2L; -.
DR   AlphaFoldDB; P13029; -.
DR   SMR; P13029; -.
DR   BioGRID; 4263062; 16.
DR   DIP; DIP-10053N; -.
DR   IntAct; P13029; 12.
DR   MINT; P13029; -.
DR   STRING; 511145.b3942; -.
DR   PeroxiBase; 2394; EcoCP01_K-12.
DR   SWISS-2DPAGE; P13029; -.
DR   jPOST; P13029; -.
DR   PaxDb; P13029; -.
DR   PRIDE; P13029; -.
DR   EnsemblBacteria; AAC76924; AAC76924; b3942.
DR   EnsemblBacteria; BAE77368; BAE77368; BAE77368.
DR   GeneID; 948431; -.
DR   KEGG; ecj:JW3914; -.
DR   KEGG; eco:b3942; -.
DR   PATRIC; fig|511145.12.peg.4063; -.
DR   EchoBASE; EB0506; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_6; -.
DR   InParanoid; P13029; -.
DR   OMA; MILAGNC; -.
DR   PhylomeDB; P13029; -.
DR   BioCyc; EcoCyc:HYDROPEROXIDI-MON; -.
DR   BioCyc; MetaCyc:HYDROPEROXIDI-MON; -.
DR   SABIO-RK; P13029; -.
DR   EvolutionaryTrace; P13029; -.
DR   PRO; PR:P13029; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004096; F:catalase activity; IDA:EcoCyc.
DR   GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR   GO; GO:0004601; F:peroxidase activity; IDA:EcoCyc.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:EcoCyc.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:EcoCyc.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:EcoCyc.
DR   HAMAP; MF_01961; Catal_peroxid; 1.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR30555; PTHR30555; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 2.
DR   TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..726
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000055564"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        106
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         267
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   SITE            102
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        105..226
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   252)"
FT                   /evidence="ECO:0000269|PubMed:12832453"
FT   CROSSLNK        226..252
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   105)"
FT                   /evidence="ECO:0000305|PubMed:12832453"
FT   CONFLICT        621
FT                   /note="A -> G (in Ref. 1; AAA24040)"
FT                   /evidence="ECO:0000305"
FT   HELIX           429..431
FT                   /evidence="ECO:0007829|PDB:1U2L"
FT   HELIX           447..458
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   TURN            459..461
FT                   /evidence="ECO:0007829|PDB:1U2L"
FT   HELIX           464..475
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   TURN            480..483
FT                   /evidence="ECO:0007829|PDB:1U2J"
FT   HELIX           491..493
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           497..499
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           501..503
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           506..520
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           525..543
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           561..563
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           566..570
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   STRAND          575..577
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   TURN            578..581
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           591..601
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           606..619
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   STRAND          623..625
FT                   /evidence="ECO:0007829|PDB:1U2J"
FT   HELIX           641..647
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   STRAND          651..657
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   STRAND          662..667
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   TURN            668..670
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   STRAND          673..678
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           679..686
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           688..697
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   STRAND          699..701
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   HELIX           703..718
FT                   /evidence="ECO:0007829|PDB:1U2K"
FT   TURN            719..721
FT                   /evidence="ECO:0007829|PDB:1U2K"
SQ   SEQUENCE   726 AA;  80024 MW;  24D32EBED5DE9BD6 CRC64;
     MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS NRSNPLGEDF
     DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF IRMAWHGAGT YRSIDGRGGA
     GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG
     FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS
     AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST
     YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP
     DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKS
     RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI IDLKFAIADS GLSVSELVSV AWASASTFRG
     GDKRGGANGA RLALMPQRDW DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA
     ASAAGLSIHV PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ
     QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR YEWKATDESK
     ELFEGRDRET GEVKFTASRA DLVFGSNSVL RAVAEVYASS DAHEKFVKDF VAAWVKVMNL
     DRFDLL
 
 
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