KATG_AZOC5
ID KATG_AZOC5 Reviewed; 744 AA.
AC A8IHK8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=AZC_3290;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) 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; AP009384; BAF89288.1; -; Genomic_DNA.
DR AlphaFoldDB; A8IHK8; -.
DR SMR; A8IHK8; -.
DR STRING; 438753.AZC_3290; -.
DR PeroxiBase; 6665; AZcaCP01.
DR PRIDE; A8IHK8; -.
DR EnsemblBacteria; BAF89288; BAF89288; AZC_3290.
DR KEGG; azc:AZC_3290; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_5; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000000270; 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; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 23..744
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354723"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 275
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 111
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 114..234
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 260)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 234..260
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 114)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 744 AA; 81788 MW; 7CBBA65A5AE19CFB CRC64;
MSPRARRCTD RCARMSERSM NATTETPTGK CPVAHGTGGT QNRDWWPNQL RVDLLNLHSP
KSDPLGAAFD YRAEFKKLDY EALKNDLRKL MTDSQDWWPA DFGNYGPQFV RMAWHSAGTY
RLADGRGGGG RGQQRFAPLN SWPDNVNIDK SRRLLWPIKQ KYGQKISWAD LMILTGNVAL
ETMGFRTFGF AGGREDTWEP DQDVFWGSET AWLSHRTLEK FDAPLGATEM GLIYVNPEGP
DRNGDPISAA KFIRETFARM AMNDEETVAL IGGGHTFGKT HGAAAESHKG PDPEAAALEA
QGLGWASNYG TGHGADTIGS GLEVTWTQTP AQWSNFFFEN LFKYEWVQTR SPAGAIQWEA
KDGPDIIPDA HNPEKKHKPT MLTTDLSLRF DPIYEKISRR FLENPQAFAE AFARAWFKLT
HRDLGPRSRY LGPEVPREVL LWQDPVPAVD HPLIDDADAA ALKAKVLASG LTVSELVGTA
WASASTFRGG DKRGGANGAR IRLAPQKDWA VNQPEQIDKV LKALTRIQGE FNLNASDGKK
VSLADVIVLA GNAGVEEAAK AAGHDVSVPF APGRTDASQA ETDADSFKWL EPAADGFRNY
QKDGLAVPAE VALIDKAQLL TLTAPELTVL IGGLRAININ VDGAKHGVFT DKPGALTTDF
FTNLLDMSTQ WKAAGESNDV YEGRDRQTGE LKWTGTRVDL VFGSNSILRA LAEVYAASDA
KDKFVTDFVA AWTKVMNLDR FDLA
