ID A0A0P0DWH9_9MICO Unreviewed; 763 AA.
AC A0A0P0DWH9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AOA12_15810 {ECO:0000313|EMBL:ALJ21285.1};
OS Microbacterium sp. No. 7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ21285.1, ECO:0000313|Proteomes:UP000059097};
RN [1] {ECO:0000313|EMBL:ALJ21285.1, ECO:0000313|Proteomes:UP000059097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ21285.1,
RC ECO:0000313|Proteomes:UP000059097};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a polypropylene glycol-degrading strain
RT Microbacterium sp. No. 7.";
RL Submitted (SEP-2015) 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}.
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DR EMBL; CP012697; ALJ21285.1; -; Genomic_DNA.
DR RefSeq; WP_054684776.1; NZ_CP012697.1.
DR AlphaFoldDB; A0A0P0DWH9; -.
DR STRING; 1714373.AOA12_15810; -.
DR KEGG; mio:AOA12_15810; -.
DR PATRIC; fig|1714373.3.peg.3252; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000059097; 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 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:UP000059097}.
FT DOMAIN 145..453
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 289
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 122
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 248..274
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 125)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 763 AA; 83332 MW; E6652549C0DB384D CRC64;
MTEQHDAVAP VGEDVTGIDQ SVTVTDTDEA QAEQAATCPV IHAQPHPTSG SANNVWWPNQ
LNLRILKKNP AVGNPLGEDF DYRAAFDSLD LAAVKADIAE TLTTSQDWWP ADFGHYGPLI
VRMAWHSAGT YRVTDGRGGG GAGQQRFAPL NSWPDNVGLD KARRILWPVK KKYGQSISWG
DLMILAGNVA LETMGFRTFG FAGGRADVWE PDDDVYWGPE TTWLGDERYS GDRELERPLA
AVQMGLIYVN PEGPNANPDP VAAARDIRET FGRMAMNDEE TVALIAGGHT FGKTHGAAHD
SNLEDNPEAA GLEMQGLGWK NNHGTGKGDD QITSGLEVTW TYHPTRWDNE FFHILYAYDW
ELFHSPAGAQ QWRPINGGGA DMVPLAHSNG RREPRMLTTD LALRFDPEYD RISRRFKDDP
EAFADAFARA WFKLTHRDMG PVERYLGPEV PAEELLWQDR VPAVDHELIA AADAAALKQQ
VLDSGLTVSE LVSVTWAAAS TFRGSDKRGG VNGARIRLAP QKDWEVNAPA QVQKVLGVLS
GIQSAFNESR TDGTRVSLAD LIVLAGNAAV EKAASDAGVD AVVPFHPGRT DASQEQTDVE
SFGYLEPAAD GFRNYYGPVA AAWGLPAEHM LIDRANLLTL SAPELTVLVG GLRVLGTNWD
GSEYGVFTDR VGVLTNDFFV NLLDLGTTWT PLDPGKHAFE GRKDGSGELV GRGTRVDLLF
GSNSELRALA EVYASDDARE KFVRDFVAAW GKVTELDRFD LHA
//
