ID A0A1U7DC18_9RHOB Unreviewed; 731 AA.
AC A0A1U7DC18;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=Ga0080559_TMP4872 {ECO:0000313|EMBL:APX25668.1};
OS Salipiger profundus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX25668.1, ECO:0000313|Proteomes:UP000186559};
RN [1] {ECO:0000313|EMBL:APX25668.1, ECO:0000313|Proteomes:UP000186559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2016 {ECO:0000313|EMBL:APX25668.1,
RC ECO:0000313|Proteomes:UP000186559};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
RL Submitted (MAR-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}.
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DR EMBL; CP014796; APX25668.1; -; Genomic_DNA.
DR RefSeq; WP_076625154.1; NZ_FOLR01000012.1.
DR AlphaFoldDB; A0A1U7DC18; -.
DR STRING; 1229727.Ga0080559_TMP4872; -.
DR KEGG; tpro:Ga0080559_TMP4872; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000186559; 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 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; 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:UP000186559}.
FT DOMAIN 156..432
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 273
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 101
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 232..258
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 104)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 731 AA; 80632 MW; F96389F818A38893 CRC64;
MDGHTVEGDL NESSRGKCPV MHGGLTALST TVMDWWPNAL NLDILHQQDA KTKPYGADFN
YREELEKLDV EALKDDLRKL MNDSQEWWPA DWGSYVGMFA RVAWHAAGSY RLADGRGGGG
TGNQRFAPLN SWPDNVNTDK GRRLLWPIKK KYGNKISWAD LMILSGTIAY EVAGLKTFGF
AFGREDIWHP EKDTYWGAEK EWLAPSDTRY GDVSKPETME NPLAAVQMGL IYVNPEGVNG
EPDPQKTADQ VRETFARMAM DDVETAALTA GGHTIGKCHG NGSADDLSPE PEAAGPEYQG
IGWMNTKGRG VGRDTVVSGI EGAWTKEPTK FDMGWFEMLF GHEWELKKSP AGAFQWMPVD
IKEEDMPVDV EDPSIKVMPI MTDADMAMKV DPVYNEICQK FMADPKYFED AFARAWFKLT
HRDMGPKARY FGPDVPQEDL VWQDPVPAGS TDYDVAAVKA KIADAGLSLS DMVSTAWDSA
RTYRGSDMRG GANGARIRLA PQKDWAGNEP ERLSAVLAKL EPIAAETGAS IADVIVLAGN
LGVERAAKAA GFDIEVPFTP GRGDATDEMT DAESFEPLEP LADGFRNWQK EDYVVSPEEM
LLDRAQLMGL TASEMTVLIG GMRAMGTNHG GSELGVFTDR KGALTTDFYD VLTDMRYQWV
PVAGGTYEIR DRKSGEVKYT ASRVDLVFGS NSILRAYAEV YAQDDNAGKF VQDFVAAWTK
VMDADRFDVA A
//
