KATG_MARSD
ID KATG_MARSD Reviewed; 727 AA.
AC C6C1T6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=Desal_1269;
OS Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS VKM B-1763) (Desulfovibrio salexigens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Maridesulfovibrio.
OX NCBI_TaxID=526222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001649; ACS79332.1; -; Genomic_DNA.
DR RefSeq; WP_015851150.1; NC_012881.1.
DR AlphaFoldDB; C6C1T6; -.
DR SMR; C6C1T6; -.
DR STRING; 526222.Desal_1269; -.
DR EnsemblBacteria; ACS79332; ACS79332; Desal_1269.
DR KEGG; dsa:Desal_1269; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_7; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000002601; 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..727
FT /note="Catalase-peroxidase"
FT /id="PRO_1000216222"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 260
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 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 96..219
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 245)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 219..245
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 727 AA; 80299 MW; 003B3CF4A23E37CF CRC64;
MSDEKKCPVT GRTSSQVAGS GTSNKDWWPN QLNLNILHQH SAKSDPMGKD FNYAEEFKKL
DLEALKKDLF ELMTDSQDWW PADYGHYGPF FIRMAWHSAG TYRIGDGRGG AGSGSQRLAP
LNSWPDNVNL DKARRLLWPI KKKYGRKISW ADLMIFAGNC AIESMGLKPF GFAGGREDIW
EPEEDIYWGD EDTWLGDTRY SGDRKLDNPL AAVQMGLIYV NPEGPNGDPN AVASGKDVRE
TFARMAMNDE ETVALVAGGH TFGKCHGAGD AANVGPDPEG APIEQQGLGW KSKFGSGKGG
DTISSGIEGA WTPTPIKWDN SYFDTLFGYE WNLEKSPAGA WQWHPSDPEA KKAVPDAHDP
SKTHPPMMTT ADLSLRMDPI YAPIAKRFHE NPEEFADAFA RAWFKLTHRD MGPRARYLGS
MVPDEELIWQ DPVPAVDHEL IDNTEIADLK AKILASGLSI SKLVSAAWAS ASTYRDSDKR
GGSNGARIRL APQKDWYVNQ PLQLPELLNK LEEIQQHFNS KSGNKKVSLA DLIVLGGCAA
VEQGAKNAGF DVTVPFTPGR TDASQEQTDV HSFAVLEPAA DGFRNYQKVK YSVTPEELLV
DKAQLMTLTA PEMTVLIGGM RVLDANFDGS KHGVFTDKPG SLNNDFFSNL LDMDTVWTST
SEDAELFEGR DRESGELKWS ATRIDLIFGA NSQLRAIAEV YGCEDSGEKF VNDFISAWDK
VMNLGIF
