KATG2_SHESM
ID KATG2_SHESM Reviewed; 739 AA.
AC Q0HES2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961};
GN OrderedLocusNames=Shewmr4_3379;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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 -!- 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; CP000446; ABI40445.1; -; Genomic_DNA.
DR RefSeq; WP_011624112.1; NC_008321.1.
DR AlphaFoldDB; Q0HES2; -.
DR SMR; Q0HES2; -.
DR PeroxiBase; 3614; SHspCP01_MR-4.
DR KEGG; she:Shewmr4_3379; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 27..739
FT /note="Catalase-peroxidase 2"
FT /id="PRO_5000130194"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 268
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 102
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 105..227
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 253)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 227..253
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 105)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 739 AA; 81223 MW; 6F90A9998479C18C CRC64;
MKKTTIPTLS ALTLAMSLAF GGAAIAQEQV TGNQFWWPEQ LNLSPLRQNA VESNPYGSDY
HYAEAFKSLD LDAVKKDIKA LMTESQDWWP ADYGHYGPFF IRMAWHSAGV YRIFDGRGGA
AGGQQRFEPL NSWPDNVNLD KARRLLWPIK QKYGSKISWG DLMVFTGNVA LESMGFKTFG
FAGGRVDDWE AEQVNWGSEK AWLDSKRRNE KGELAKPMGA TQMGLIYVNP EGPNGVPDPL
ASAKEIRDTF GRMAMNDEET VALIAGGHTF GKAHGAHDPS KCVGADPAAS GVEAQGLGWK
NKCGKGHSED TVTSGLEGAW SSNPTKWTME YLTWLYTFDW VQTKSPAGHI QWIPADGKAA
NLIPDAHIAD KRHAPMMFTS DIALKEDPIY REITTRFLKN PQEFELAFAK AWFKLTHRDM
GPKARYLGAD VPAEMLIWQD PIPALDHLVI DNADIKALGN KILASGLTVP ELVRTAWASA
SSFRGTDMRG GANGARIRLE PMMNWQANNP KELAKVLAKL EKVQKDFNGS LKGGKKVSLA
DVIVLGGSVA VEKAAKEAGV AVSVPFTPGR MDATQAQTDV SSFAVLEPTA DGFRNYYSKD
SSHSPAEMLI ERANMLNLTV PEMTVLVGGL RALDANSAGV KHGVFTDKPG TLSNDFFVNL
LDMSTKWSKS EKQEGIYEGQ DRKSGKLKWT ATPVDLVFGS HSELRAVSEV YGAQDGQDRF
VQDFIKAWNK VMNADRFDI
