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KATG_ARCFU
ID   KATG_ARCFU              Reviewed;         741 AA.
AC   O28050;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
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=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=perA;
GN   OrderedLocusNames=AF_2233;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   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).
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.
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:0000255|HAMAP-Rule:MF_01961};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
CC         {ECO:0000269|PubMed:18178143};
CC         KM=3.8 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC         {ECO:0000269|PubMed:18178143};
CC         KM=95 mM for H(2)O(2) for the peroxidase reaction
CC         {ECO:0000269|PubMed:18178143};
CC         KM=16 mM for ABTS for the peroxidase reaction
CC         {ECO:0000269|PubMed:18178143};
CC         Vmax=11760 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         Vmax=5500 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC         (at pH 7.0) {ECO:0000269|PubMed:18178143};
CC         Vmax=12 umol/min/mg enzyme for ABTS for the peroxidase reaction
CC         {ECO:0000269|PubMed:18178143};
CC       pH dependence:
CC         Optimum pH is 4.5 for the peroxidase reaction.
CC         {ECO:0000269|PubMed:18178143};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
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   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR   EMBL; AE000782; AAB89022.1; -; Genomic_DNA.
DR   PIR; A69529; A69529.
DR   RefSeq; WP_010879722.1; NC_000917.1.
DR   AlphaFoldDB; O28050; -.
DR   SMR; O28050; -.
DR   STRING; 224325.AF_2233; -.
DR   PeroxiBase; 1858; AfCP01.
DR   EnsemblBacteria; AAB89022; AAB89022; AF_2233.
DR   GeneID; 24795995; -.
DR   KEGG; afu:AF_2233; -.
DR   eggNOG; arCOG04487; Archaea.
DR   HOGENOM; CLU_025424_2_0_2; -.
DR   OMA; MILAGNC; -.
DR   OrthoDB; 2839at2157; -.
DR   PhylomeDB; O28050; -.
DR   BRENDA; 1.11.1.21; 414.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome.
FT   CHAIN           1..741
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000055579"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         249
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                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   SITE            83
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        86..208
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   234)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        208..234
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   86)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   741 AA;  84854 MW;  A931DF34F050FC63 CRC64;
     MMRQGGVMVG ARKRWITDWW PNRLNLKILR QNLQNPYGED YDYVEEVENL DIDAVIRDLK
     ELMRSSQDWW PADFGHYGPL FIRLAWHSAG SYRIFDGRGG ARDGSIRFPP RINWPDNINL
     DKAIRLLWPI KKKYGRKLSW ADLIILAGTV AMEDMGVKLF GFALGREDIF EPDESPDWGP
     EEEMLTAKRG EKEELERPFA ATEMGLIYVN PEGPGGNPDP LGSAQEIRVA FRRMGMNDEE
     TVALIAGGHA FGKCHGAGPA DYLGPDPSSS PIEMQGLGWK YNYGKGKGSD TFTSGLEVTW
     SPTPTKFGIN YLRILFTYEW ELEKSPAGKN QWVAKDAPEI IPDAHDPNKK HRPRMLTADL
     ALRFDPEFSK IARRFLENPE EFEKAFAIAW YKLTHRDMGP KDCYIGKYVP EETFVWQDPL
     PRRDYELVDE KDVEELKRRI LASGLSLSQL VYFAWASAST YRNSDRRGGA NGARIRLKPM
     SVWEVNHPEE LKKVIAAYEK IQQEFNEGAK GSEKRISIAD LIVLGGIAAV EEAARRAGFS
     VKVPFIPGRV DAQQEHVDEE FYRVIEPFAD GFRNYFRYPE RINERDVYTT PEYFLVDKAN
     LLTLTVPEMV VLIGGMRALG ANYSHSDYGV LTERPGVLSN DFFVNLLDMS VEWRAADDYR
     YTFEGYDRKS GELRWRATRV DLILGHHDEL RAVAEVYGCD DAKEKFVKDF AAVCAKVMHL
     DRFDLWRSNR KLYKEITAGL R
 
 
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