ID   C1DB78_LARHH            Unreviewed;       724 AA.
AC   C1DB78;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Catalase-peroxidase {ECO:0000256|ARBA:ARBA00074141, ECO:0000256|HAMAP-Rule:MF_01961};
DE            Short=CP {ECO:0000256|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000256|ARBA:ARBA00067012, ECO:0000256|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961};
GN   Name=katG {ECO:0000256|HAMAP-Rule:MF_01961};
GN   OrderedLocusNames=LHK_02436 {ECO:0000313|EMBL:ACO75418.1};
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO75418.1, ECO:0000313|Proteomes:UP000002010};
RN   [1] {ECO:0000313|EMBL:ACO75418.1, ECO:0000313|Proteomes:UP000002010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9 {ECO:0000313|EMBL:ACO75418.1,
RC   ECO:0000313|Proteomes:UP000002010};
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA   Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA   Pallen M.J., Lok S., Yuen K.Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
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 = O2 + 2 H2O; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00049145, ECO:0000256|HAMAP-
CC         Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O2 + AH2 = 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADH + O2 + H(+) = H2O2 + NAD(+); Xref=Rhea:RHEA:11264,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU10012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + O2 + H(+) = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU10012};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|HAMAP-
CC         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|ARBA:ARBA00060838, ECO:0000256|HAMAP-
CC       Rule:MF_01961, ECO:0000256|RuleBase:RU003451}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}.
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DR   EMBL; CP001154; ACO75418.1; -; Genomic_DNA.
DR   RefSeq; WP_012697904.1; NC_012559.1.
DR   AlphaFoldDB; C1DB78; -.
DR   STRING; 557598.LHK_02436; -.
DR   KEGG; lhk:LHK_02436; -.
DR   eggNOG; COG0376; Bacteria.
DR   HOGENOM; CLU_025424_2_0_4; -.
DR   Proteomes; UP000002010; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:TreeGrafter.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   CDD; cd00649; catalase_peroxidase_1; 1.
DR   FunFam; 1.10.420.10:FF:000004; Catalase-peroxidase; 1.
DR   FunFam; 1.10.520.10:FF:000002; Catalase-peroxidase; 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   NCBIfam; NF011635; PRK15061.1; 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:UP000002010}.
FT   DOMAIN          132..426
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01961,
FT                   ECO:0000256|PROSITE-ProRule:PRU10012"
FT   BINDING         267
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            95
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT   CROSSLNK        226..252
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT                   98)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   724 AA;  80054 MW;  87921CB97BDB4921 CRC64;
     MESKGVNVAG KCPVMHGGLT SASMSNMDWW PKALNLDILH QHDSKTNPMG AGFNYREEVR
     KLDVEALKAD LKALMTDSQD WWPADWGHYG GLMIRMAWHS AGTYRTADGR GGGGTANQRF
     APINSWPDNA NLDKARRLLW PVKKKYGNKI SWADLIILAG TMAYESMGLK TFGFGFGRED
     IWHPEKDTYW GSEKEWLAPS GSEGSRYSGE RDLENPLAAV MMGLIYVNPE GVDGQPDPLK
     TARDMRITFA RMAMDDEETV ALTAGGHTVG KCHGNGNAAN LGPAPEGAGL EEQGLGWMNH
     TTRGCGRDAV TSGIEGAWTT HPARWDNGYF SMLLDHDWWL HKSPAGAWQW EPVSIREEDM
     PVDVEDPSIR RKPIMTDADM ALKFDPEYRR IADRFRQDQA YFSEVFARAW FKLTHRDMGP
     KARYIGPDVP AEDLIWQDPV PSGRKDYDVA AVKAKIAAAG LSVSDMVSTA WDSARTFRGS
     DKRGGANGAR IRLAPQKDWE GNEPARLARV LAVYETVARE CGVSVADVIV LGGSLGIEQA
     AAAAGISIHV PFSPGRGDAT DEMTDAASFD VLEPLADGFR NWLKKDYVVS AEELLLDRAQ
     LMRLTACEMT VLVGGMRVLG TNHGGTQHGV LTDRVGVLSN DFFVNLTDMA FSWQPAGSNL
     YEIRDRRTGT VKWTASRVDL VFGSNSVLRA YAEVYAQDDN REKFVRDFVA AWVKVMNADR
     FDLN
//