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
