ID A0A1V2GV14_9PROT Unreviewed; 738 AA.
AC A0A1V2GV14;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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};
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961};
GN ORFNames=BKE38_26960 {ECO:0000313|EMBL:ONG45013.1};
OS Pseudoroseomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG45013.1, ECO:0000313|Proteomes:UP000188879};
RN [1] {ECO:0000313|EMBL:ONG45013.1, ECO:0000313|Proteomes:UP000188879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|EMBL:ONG45013.1,
RC ECO:0000313|Proteomes:UP000188879};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Roseomonas sp. strain M3.";
RL Submitted (OCT-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}.
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:ONG45013.1}.
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DR EMBL; MLCO01000368; ONG45013.1; -; Genomic_DNA.
DR RefSeq; WP_076960341.1; NZ_MLCO01000368.1.
DR AlphaFoldDB; A0A1V2GV14; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000188879; 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; 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 NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF6; 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; 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:UP000188879}.
FT DOMAIN 133..411
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 480..738
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 265
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 96
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 224..250
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 99)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 738 AA; 80618 MW; 97D94697CF338170 CRC64;
MDTNATGPLG CPMKKPGATR ALLGRTNRDW WPNQLSLDIL HQKGLTGNPM GDDFDYRKEF
LSLDYAAVKR DLTALMTDSQ PWWPADYGHY GPFFIRMAWH SAGTYRTGDG RGGSSSGSQR
FAPLNSWPDN ANLDKARRLL WPIKQKYGRK LSWADLLILT GNVAIESMGG PTFGFGGGRE
DIFEPEKDIY WGTEEEWLGQ TRIDPAKEMV LESPLAAIQM GLIYVNPEGP GGVPDPVQSG
RDIRETFARM GMNDEETVAL TAGGHTFGKC HGAGDASKVG SDPEGSDIAQ QGLGWQSGHE
SGFGDHTITS GLEGAWTPDP TRWDNGYFHM LLDYEYELVR SPAGAQQWQP VNQKPEDMAP
GAHSPDRRLP TMMTTADMAM REDPAYRKIS ESFRADPAKF ADAFARAWFK LCHRDMGPKV
RYLGPEVPAE DLIWQDPIPK ADYAAIDAAD VAALEKQILA SGLSTAELVA TAWASAATFR
GSDHRGGANG ARIRLAPQKD WDVNQPDRLA KVLAVYEDIK AGFDASAKGG KKVSIADLIV
LGGSAAVEQA AKAAGHAVRV PFAPGRTDAT AAQTDVENMS VLEPKADGFR NYLQVPFNVP
TEELLLDRAQ LLGLSAPEMT VLVGGLRVLG ANHNGEKHGV LTERPGQLTN DFFVNLLDMN
TAWKLVDGAA DESFAGTDRR THQQKWTATR TDLVFGSNSQ LRALSEVYAA SDAEKKFVDD
FVAAWVKVMN ADRYDLRA
//
