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Database: UniProt
Entry: I5CAG7_9BACT
LinkDB: I5CAG7_9BACT
Original site: I5CAG7_9BACT 
ID   I5CAG7_9BACT            Unreviewed;       725 AA.
AC   I5CAG7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   13-SEP-2023, entry version 48.
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=A3SI_02191 {ECO:0000313|EMBL:EIM78819.1};
OS   Nitritalea halalkaliphila LW7.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Nitritalea.
OX   NCBI_TaxID=1189621 {ECO:0000313|EMBL:EIM78819.1, ECO:0000313|Proteomes:UP000005551};
RN   [1] {ECO:0000313|EMBL:EIM78819.1, ECO:0000313|Proteomes:UP000005551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LW7 {ECO:0000313|EMBL:EIM78819.1,
RC   ECO:0000313|Proteomes:UP000005551};
RA   Jangir P.K., Singh A., Shivaji S., Sharma R.;
RT   "Genome sequence of Nitritalea halalkaliphila LW7.";
RL   Submitted (MAY-2012) 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:EIM78819.1}.
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DR   EMBL; AJYA01000002; EIM78819.1; -; Genomic_DNA.
DR   RefSeq; WP_009053368.1; NZ_AJYA01000002.1.
DR   AlphaFoldDB; I5CAG7; -.
DR   STRING; 1189621.A3SI_02191; -.
DR   PATRIC; fig|1189621.3.peg.459; -.
DR   OrthoDB; 9759743at2; -.
DR   Proteomes; UP000005551; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000005551}.
FT   DOMAIN          131..422
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT   BINDING         263
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            94
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT   CROSSLNK        222..248
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT                   97)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   725 AA;  80489 MW;  C1B445C820923C22 CRC64;
     MEQRSKSGGK CPVMHGANTV QEKNVMEWWP NALNLDILHQ HDEKTKPYGA DFSYKDAFLS
     LDLEAVKSDL KALMTDSQDW WPADWGTYGG LMIRMAWHAA GTYRVADGRG GANTGNQRFA
     PLNSWPDNTN LDKARRLLWP IKKKYGNALS WADLFVLAGN MAYESMGFKT FGFAGGREDI
     WHPEKDINWG SEREWLGKSR YADASADSLA NPLAAVQMGL IYVNPEGVDG NPDPLKTAHD
     VRTTFARMAM NDEETVALTA GGHTVGKTHG NGLEAHLGPN PEGADVEEQG FGWKNPKGSG
     HGADTVTSGL EGAWTTTPDR WNHTYFHLLL NHEWELTKSP AGAWQWEPVA MKEEDKPFDA
     HIPGVRRNPI MTDADMAMKM DPAYRKISQR FYEDPAYFED VFARAWFKLT HRDLGPKSRY
     LGADVPQEEL IWQDPVPTVG YTLSEAEITA LKASLLQLDV APADFISTAW DSARTFRGSD
     YRGGANGARI RLEPQRSWEG NEPERLERVL TALTEFQAGL EKKISLADLI VLAGTAAVEQ
     AARKAGVSLT VPFSPGRGDA TAEQTDAESF SYLEPVHDGF RNWLKPGVEA KAEELLVDRA
     QLMGLTAAEM TALVGGMRVL GTNYGGTEKG VFTDRVGVLS TDFFVHLTDM AYSWKSTGAD
     SYALVDRKTG EEAFTASRVD LVFGSNSILR AYAEYYAQDD MAERFVQDFC RAWVKVMDAD
     RFDLK
//
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