KATG_ACIAC
ID KATG_ACIAC Reviewed; 743 AA.
AC A1TRV8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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}; OrderedLocusNames=Aave_3132;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000512; ABM33696.1; -; Genomic_DNA.
DR RefSeq; WP_011796206.1; NC_008752.1.
DR AlphaFoldDB; A1TRV8; -.
DR SMR; A1TRV8; -.
DR STRING; 397945.Aave_3132; -.
DR PeroxiBase; 5384; AavCP01.
DR PRIDE; A1TRV8; -.
DR EnsemblBacteria; ABM33696; ABM33696; Aave_3132.
DR KEGG; aav:Aave_3132; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000002596; 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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..743
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354710"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 277
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 90
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 93..236
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 262)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 236..262
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 93)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 743 AA; 81229 MW; F39D462DCA067D92 CRC64;
MTQDATKCPF HAAAASGGII NKDWWPNQLR LDLLNQHSSK SDPLGAGFDY AEEFKKLDYE
GLKRDLRALM TDSQDWWPAD FGHYGPQFVR MTWHAAGTYR TGDGRGGAGR GQQRFAPLNS
WPDNVNIDKS RRLLWPIKQK YGQKISWADL LVLTGNVALE TMGFRTFGFA GGREDTWEPD
QDVYWGSEKT WLGGDARYGK GTPGDGTLVA EPAMHGHEKD RVLENPLAAV QMGLIYVNPE
GPEGNPDPVA AAHDIRETFA RMAMNDEETV ALIAGGHTFG KTHGAGTADH VGPEPEAAGL
EQQGLGWASS FGSGKAGDAI TSGLEVTWTS TPAQWGNEFF ENLFKFEWEL TKSPAGAHQW
QAKNAPATIP DAHDPSKKRV PTMLTTDLSL RFDPAYEKIS RRFLENPQAF AEAFARAWFK
LTHRDMGPRA RYLGPEVPKE ELVWQDPIPA VTHDLVDAAD VAALKARVLA SGLTVQELVG
TAWASASTFR GSDKRGGANG ARIRLAPQKD WAVNQPEQLA RVLQVLEGIQ REFNKGADGD
KRISLADLIV LAGAAGVEQA ARAAGVAVTV PFHPGRADAR QDQTDVESFS VLEPSADGFR
NYTKARYSVP AEVLLLDKAQ LLTLTAPEMT VLVGGLRAIN INVGGATHGV FTATPGALTN
DFFANLLDMS TEWKPAGDLF EGRDRKTGEK RWTGTRVDLV FGSNSVLRSL AEVYASADAK
EKFVRDFVAA WAKVMDLDRF DLR
