KATG2_IDILO
ID KATG2_IDILO Reviewed; 751 AA.
AC Q5QWH3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=IL1414;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017340; AAV82254.1; -; Genomic_DNA.
DR RefSeq; WP_011234660.1; NC_006512.1.
DR AlphaFoldDB; Q5QWH3; -.
DR SMR; Q5QWH3; -.
DR STRING; 283942.IL1414; -.
DR PeroxiBase; 2635; IlCP01.
DR EnsemblBacteria; AAV82254; AAV82254; IL1414.
DR KEGG; ilo:IL1414; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001171; 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 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 PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
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; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 28..751
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000354811"
FT ACT_SITE 116
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 279
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:0000255|HAMAP-Rule:MF_01961"
FT SITE 112
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 115..238
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 264)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 238..264
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 115)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 751 AA; 83425 MW; 4FAF10E9893609AC CRC64;
MFKKTVPLLS AVAIAISFSA GTGVANAQEN ASYEVNSPEP KSNDFWWPNK LNLEPLRQHS
PESDPYGDDF DYAEAFSQLD LEQVKKDIEE LMTSDQDWWP ADYGHYGPFF IRMAWHGAGT
YRVQDGRGGA AGAQQRFEPL NSWPDNVSLD KARRLLWPVK QKYGRDISWA DLMVLTGNVA
LESMGFETFG FAGGREDAWE PDIVYWGPEK EWLKGDERYS GDRELENPLA AVQMGLIYVN
PEGPNGKPDP LLAAKDIRDT FGRMAMNDEE TVALIAGGHT FGKAHGAHKP EECLGAEPAA
AGVEEQGLGW KNKCGKGNAE DTITSGLEGA WSVNPTAWTT QYLDNLFGFE WEQTKSPAGA
IQWIPVDGQA SNLVPDAHVE GKRHAPIMFT TDLSLKEDPE YRKIAKRFHE DPKEFELAFA
KAWFKLTHRD MGPKQSYLGD MAPQEDLLWQ DPIPAVDFEL INENDVEQLK VAILDSGLSV
PQLVRTAWAS ASSFRGTDMR GGANGARIAL EPQMNWEANN PAELKKVLDT LKGVQEDFND
ELSGDKYVSL ADVIVLGGAA AIEKAGKDAG YDVTVPFEPG RTDASQEMTD VNSFSFLEPK
ADAFRNYYAE GNRVSPAQHM VDKADQLTLT VPEMTVLVGG LRSLDANYND SDHGVFTDQP
GTLNNDFFVN LLSMDNEWKK SSDNEAIYEG FDRKTGEQKY TATTVDLIFG SNSELRAVAE
VYAMSDADEK FVNDFVQAWT KVMQLDRFDL K
