KATG_SALRD
ID KATG_SALRD Reviewed; 729 AA.
AC Q2RZX7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=SRU_2405;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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}.
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DR EMBL; CP000159; ABC45695.1; -; Genomic_DNA.
DR RefSeq; WP_011405122.1; NC_007677.1.
DR RefSeq; YP_446504.1; NC_007677.1.
DR AlphaFoldDB; Q2RZX7; -.
DR SMR; Q2RZX7; -.
DR STRING; 309807.SRU_2405; -.
DR PeroxiBase; 3063; SruCP01.
DR EnsemblBacteria; ABC45695; ABC45695; SRU_2405.
DR KEGG; sru:SRU_2405; -.
DR PATRIC; fig|309807.25.peg.2505; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_10; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000008674; 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.
FT CHAIN 1..729
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354901"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 255
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..214
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 240)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 214..240
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 729 AA; 82038 MW; 4D127EFC5C88E187 CRC64;
MHNGSNGSVE QRDSMPETSR EWWPGSLDVE ILDQNAQDVG PWNGDFDYAE AFQELDYEAL
KEDIEEVMTT SKDWWPADYG HYGPLFIRMS WHAAGTYRTT DGRGGSSGGR QRLAPLNSWP
DNANLDKARR LLWPVKQKYG RKISWADLLV LAGNVAMESM GFETFGFAGG REDDFKPDES
IDWGPEDEME TWGRFNEEDE LDNPLGATVM GLIYVNPEGP ESTPDPEWSA QRIRKSFGRM
AMNDRETAAL IAGGHTFGKV HGADTDEHLQ AEPEAAPIEQ QGLGWHNEHG SGKGGDTITS
GIEGPWTDAP TEWDMGYLDF LLDYEWEVHK GPGGAWQWRP KSDELKGVVP DAHDASETVD
PMMLTTDVAL KRDPDYREII EDFRENPDAF EDAFARAWFK LLHRDMGPKE RYLGPEVPEE
DLIWQDPVPD ADHDLIGDEE IAELKEAILE TDLSVSRLVK TAWASASTYR DSDKRGGANG
ARIRLEPHRN WEANEPPQLA HALEVLTGIQ KNFNDARTDD VRVSLADLIV LGGSAAIEKA
AADAGHDVEV PFTPGRTDAT QEQTDVEAFE YLEPKADGFR NYIADDPWQD WTPEEFLVDK
ADLLNLTPAE TTVLVGGMRA LDATHEQADG YGVFTDRPET LNNDYFVNLL DMGHEWDPVS
EDKQHFKIRD RDTGEVKWKA TRVDLIFGSN SRFRALSQVY GSGDAEEKFV DDFVDAWTKV
MNLDRFDLE
