ID F1VW85_9BURK Unreviewed; 747 AA.
AC F1VW85;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=IMCC9480_1113 {ECO:0000313|EMBL:EGF33140.1};
OS Oxalobacteraceae bacterium IMCC9480.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae.
OX NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF33140.1, ECO:0000313|Proteomes:UP000004494};
RN [1] {ECO:0000313|EMBL:EGF33140.1, ECO:0000313|Proteomes:UP000004494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF33140.1,
RC ECO:0000313|Proteomes:UP000004494};
RX PubMed=21572000; DOI=10.1128/JB.05088-11;
RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT betaproteobacterium isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3421-3421(2011).
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:EGF33140.1}.
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DR EMBL; AEPR01000109; EGF33140.1; -; Genomic_DNA.
DR AlphaFoldDB; F1VW85; -.
DR Proteomes; UP000004494; 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 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; 1.
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:UP000004494}.
FT DOMAIN 118..425
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 263
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 80
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 222..248
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 83)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 747 AA; 82821 MW; A16B0DE76451B71A CRC64;
MGGAFGTPPT LENWYPDRLR VELLHQNGLA ADPLGPDFDY AAEFAKLDFE ALKGDIKQFL
TTSVDWWPSD YHNYGPQMVR MAWHAAGTYR IADGRGGAGT AMQRFAPISS WWDNGNTDKS
RRLLQPIKHK YGNGLSWGDL MVLTGNCALE IMGFPTYGFG GGRLDAWEAD NATYWGPEIW
DPKNVNGFDS MVTRDKRWRG NNGDADYDLE NPLAATHQAL IYVNPEGPYA NGDPMGSARD
IRISFTRMAM NDEETVALIA GGHAFGKSHG MVSPKDVGPP PEIAPMEAMG LGWANPNGPG
FAQYTMTNGI EGSWTPNPTQ WDNSYLENLF KFEWKQIKSP AGALQWTPTD PNAPKTPDAH
VEGQMNDLMM MTSDIALKVD PEFRKVCEKF LADFDAFTQA FSKAWYKLTH RDMGPRHRYL
GPEVRIEDGL LWQDPLPERR HELVCEADIV GLKQAVLATD VSVSDLVFTA FSAAATYRDS
DKRGGANGGR LALAPQKDWV VNRRAAPVVE KLRGIMADFN GALGAGKKIS LADLIVLGGC
AAVERAARES GIEATVPFTP GRVDTTQQLT DVEMFEWLKP VVDGFRNYTD ERFGQISQGV
APEEFFLDKA NLMKLSAPEW TVLTGGLRVL NANHDGSDLG IFTKRVGMLT NDFFVHLTDT
DLIWEKADTD GLSFVLKDRA SGAPRFRASR NDLVFGSNAQ LRSISDVYAS SDGHPRFVKD
FIMVWDKVMM LDRYDVKGHR RTAPMAS
//
