ID A0A1H1WMH1_9FLAO Unreviewed; 742 AA.
AC A0A1H1WMH1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN04489797_2915 {ECO:0000313|EMBL:SDS97801.1};
OS Winogradskyella sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS97801.1, ECO:0000313|Proteomes:UP000198963};
RN [1] {ECO:0000313|EMBL:SDS97801.1, ECO:0000313|Proteomes:UP000198963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA_55 {ECO:0000313|EMBL:SDS97801.1,
RC ECO:0000313|Proteomes:UP000198963};
RA Varghese N., Submissions S.;
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}.
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DR EMBL; LT629774; SDS97801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1WMH1; -.
DR STRING; 1249933.SAMN04489797_2915; -.
DR Proteomes; UP000198963; Chromosome I.
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 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}.
FT DOMAIN 150..471
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 285
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 113
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 244..270
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 116)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 742 AA; 82832 MW; D19E4DD937724F2F CRC64;
MEKSTHDSAD PIHAENEELN PHGGSGTGKC PFMQGAITTT EKSVTDWWPN TLNLDILHQH
DTKTNPLGAD FNYQEELKKL DVDALKKDLH DFMTDSQDWW PADWGHYGGL MIRMAWHAAG
SYRLADGRGG GGTGNQRFAP LNSWPDNVSL DKARRLLWPI KKKYGNKVSW ADLIILAGTI
AYESMGLKTY GFAFGREDIW HPEKDVYWGA EKEWLAPSDE RYTNVDSPET MENPLAAVQM
GLIYVNPEGV NGKQDPLKTA QQVRETFKRM AMNDEETVAL TAGGHTVGKT HGNGDASILG
PDPESADVDA QGLGWANPTK SGKGRYTVTS GLEGAWTTHP TKWDNGFFEM LFNHEWESVK
SPAGADQWEP VSIKEEDKPV DVEDLTTRHN PMMTDADMAM KMDPIYRAIS LKFMNDFEYF
SDTFARAWFK LTHRDMGPKD RWFGPDVPQE DLIWQDPIPK GNYNYDVAAV KAKIANTDLT
ISELVSTAWD SARTFRGSDM RGGANGARIR LEPQNTWEAN EPEQLQNVLA VLEPIASEFN
ISVADTIVLA GNVGVEKAIK NAGMEVNVPF APGRGDASQE MTDVESFESL EPLADGYRNY
QKKDYVVSPE ELLLDKTQLL GLTAAEMTVL IGGMRVLGTN YGGTKHGVFT ENEGALTNDF
FVNLTDMIYE WKSQDDGTYQ ITNRHTGEVK YTATRVDLVF GSNSILRAYS ELYAQDDSKA
KFVNDFVAAW TKVMNLGRFD IK
//
