ID A0A443IAK9_9GAMM Unreviewed; 737 AA.
AC A0A443IAK9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE Short=CP {ECO:0000256|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961};
GN ORFNames=ED28_16355 {ECO:0000313|EMBL:RWR01020.1};
OS [Pantoea] beijingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1324864 {ECO:0000313|EMBL:RWR01020.1, ECO:0000313|Proteomes:UP000288794};
RN [1] {ECO:0000313|EMBL:RWR01020.1, ECO:0000313|Proteomes:UP000288794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27579 {ECO:0000313|EMBL:RWR01020.1,
RC ECO:0000313|Proteomes:UP000288794};
RA Xu F., Liu Y., Wang S., Yin Y., Ma Y., Zhao S., Rong C.;
RT "Draft genome sequence of Pantoea beijingensis strain LMG 27579, an
RT emerging pathogen to Pleurotus eryngii with potential industrial
RT application.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
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:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000256|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01961,
CC ECO:0000256|RuleBase:RU003451}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR01020.1}.
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DR EMBL; JMEE01000044; RWR01020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443IAK9; -.
DR Proteomes; UP000288794; Unassembled WGS sequence.
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 CDD; cd00649; catalase_peroxidase_1; 1.
DR CDD; cd08200; catalase_peroxidase_2; 1.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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 NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 2.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01961};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01961};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_01961}; Reference proteome {ECO:0000313|Proteomes:UP000288794};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961,
FT ECO:0000256|RuleBase:RU003451"
FT CHAIN 24..737
FT /note="Catalase-peroxidase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961,
FT ECO:0000256|RuleBase:RU003451"
FT /id="PRO_5018817672"
FT DOMAIN 136..428
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 531..737
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 264
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:0000256|HAMAP-Rule:MF_01961"
FT SITE 99
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 102..223
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with Met-
FT 249)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 223..249
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 102)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 737 AA; 80715 MW; 278129B9CA64B553 CRC64;
MFKKILPLLI TLAMTNGMSA AWADEKSPST NFYQPNTLDL SPLRLHSAES NPYGSDFNYA
KEFNSLDLAA VKKDIQAVLT TSQDWWPADY GNYGPFFIRM AWHGAGTYRT YDGRGGASGG
QQRFEPLNSW PDNVNLDKAR RLLLPIKMKY GAQISWGDLM VLTGNVALES MGFKTLGFAG
GREDDWQSDL VYWGAGNKIL SSNRDKNGHL PKPLAATQRG LIYVNPEGPN GKPDPLASAK
DIREAFGRMA MDDEETVALI AGGHTFGKAH GAASPEKCVG PAPDGAAIED QGLGWKNKCG
TGNGKDTIGS GLEGAWTSSP THFTLQYLNN LYKYDWVLNK SPAGAWQWVP KNAKNVVPDA
HDPSELHPLM MFTTDIALKV DPEYKKVTTR FLDNPEEFEL AFARAWFKLT HRDMGPKARY
LGNEIPKDNF IWQDPIPAAD YKTIESADIT TLKETILKAG LSDSDLIRTA WASASSFRVT
DYRGGDNGAR IRLLPQKNWE VNDPAKLDSI LTSLADIQNG FNKDRTDGKK VSLSDLIVLA
GNTAVEDAAK KAGYTITLPF TPGRTDAAQS DTDIESFGAL EPVADGFRNY YAKDKNTVSP
VEALIDKSGK LDLTVPEMTV LLGGLRVLDA NTGGAKEGVL TATPGQLNNS FFVNLLDMST
RWSASPKSAG LYDGVERKSG QHKWTASSVD LIFGSNPELR AVAEVYASDD AKEKFVNDFA
KAWTKVMNLD RFDLKKG
//
