ID S4MAP7_9ACTN Unreviewed; 741 AA.
AC S4MAP7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=STAFG_6495 {ECO:0000313|EMBL:EPJ36488.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ36488.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ36488.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ36488.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPJ36488.1}.
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DR EMBL; AOPY01001562; EPJ36488.1; -; Genomic_DNA.
DR RefSeq; WP_020275350.1; NZ_KE354328.1.
DR AlphaFoldDB; S4MAP7; -.
DR PATRIC; fig|1283301.3.peg.6445; -.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000015001; Unassembled WGS sequence.
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 InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF0; 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; PS00435; PEROXIDASE_1; 1.
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:UP000015001}.
FT DOMAIN 143..430
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
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 106
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 109)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 741 AA; 81231 MW; 06F2527F90BD6A2A CRC64;
MTENHDAIVT DAKQEETSGG CPVAHGRALH PTQGGGNRQW WPERLNLKIL AKNPEVANPL
GEEFDYAEAF QALDLAAVKQ DIAEVLTTSQ DWWPADFGNY GPLMVRMAWH SAGTYRISDG
RGGAGAGQQR FAPLNSWPDN GNLDKARRLL WPVKKKYGQS ISWADLMILT GNVALEQMGF
ETFGFAGGRE DVWEPEEDVY WGPETTWLDD KRYTGDRELE NPLGAVQMGL IYVNPEGPNG
NPDPLAAARD IRETFRRMAM NDEETVALIA GGHTFGKTHG AGPADHVGAD PEAASMEEQG
LGWRSTYGTG KGGDAITSGL EVTWTSTPTQ WSNGFFKNLF EFEYELEQSP AGANQWVAKD
APEIVPDAHD SSKKHRPKML TTDLALRFDP IYEPISRRFY ENPQEFADAF ARAWFKLTHR
DMGPKSLYLG PEVPEETLIW QDPLPEAEGE PIDAGDIATL KTKLLESGLS VSQLVTTAWA
SASTFRGSDK RGGANGARIR LEPQRGWEVN EPDELAQVLR VLENIQQEFN AGAGAKKVSL
ADLIVLGGTA AVEKAAKEAG FQVEVPFTPG RVDATEEHTD AESFEALEPT ADGFRNYHGK
GNRLPAEYLL LDRANLLTLS APEMTVLVGG LRVLGANYQQ SQLGALTATP GSLTNDFFVN
LLDLGTTWKA TSEDQTTFEG RDAATGEVKW AGSRADLVFG SNSELRALAE VYASDDAKEK
FVNDFVAAWV KVMNLDRFDL V
//
