ID A0A4Z0M0E7_9GAMM Unreviewed; 737 AA.
AC A0A4Z0M0E7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961,
GN ECO:0000313|EMBL:TGD72765.1};
GN ORFNames=E4634_14715 {ECO:0000313|EMBL:TGD72765.1};
OS Haliea sp. SAOS-164.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Haliea.
OX NCBI_TaxID=2562682 {ECO:0000313|EMBL:TGD72765.1, ECO:0000313|Proteomes:UP000298050};
RN [1] {ECO:0000313|EMBL:TGD72765.1, ECO:0000313|Proteomes:UP000298050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAOS-164 {ECO:0000313|EMBL:TGD72765.1,
RC ECO:0000313|Proteomes:UP000298050};
RA Verma A., Kumar P., Krishnamurthi S.;
RT "Taxonomy of novel Haliea sp. from mangrove soil of West Coast of India.";
RL Submitted (APR-2019) 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:TGD72765.1}.
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DR EMBL; SRLE01000009; TGD72765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z0M0E7; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000298050; 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:UP000298050};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961,
FT ECO:0000256|RuleBase:RU003451"
FT CHAIN 24..737
FT /note="Catalase-peroxidase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961,
FT ECO:0000256|RuleBase:RU003451"
FT /id="PRO_5021509504"
FT DOMAIN 139..415
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 268
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 102
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 227..253
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 105)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 737 AA; 80961 MW; 5873BFECE37B3A0C CRC64;
MKPLKTVRKA ITVATLCALG ATAAATHAEA PDNDYWWPNR LSLEPLRDAS ASADPMGADF
DYAEAFETLD VKALEKDLRA LMKDSQDWWP ADFGHYGPFF IRMSWHAAGT YRTIDGRGGA
DGGMQRFAPL NSWPDNASLD KARRLLWPIK EKYGNAVSWA DLIVLAGNMA MDDMGFKTLG
FAFGRADEWQ PEDVNWGPEG EWLTDQRRNE MGRIEGPFGA TEMGLIYVNP EGPHKNPDPL
KAAQAIRDAF GRMAMNDEET AALIAGGHTF GKAHGAHKAA DCVGPEPEAA PLEQQGLGWA
NKCGTGKGSD AVTSGLEGAW TINPVQWTHN YLQNLYGFEW ELHIGPGGAQ QWRPVDGQGA
SLVPDAHDPD KRHAPMMFTT DIALKEDPSY RKITQRWLEN PEEFEQAYAR AWFKLIHRDM
GPASRYLGPW APEESFIWQD PVPEADYKQV SDKDISRLKS EILDTGLSVG ELVRTAWASA
STFRETDMRG GANGARIRLM PQKDWAVNEP ADLAKVLAKL EKVQADFNKK SRKTKVSLAD
VIVLGGAAAI EKAAADAGYK VSVPFVPGRT DATQEMTEVA SFTVLEPKSD GFRNYHAASY
DHPPAQALVE KAALLDLTVP EMTALVGGMR VLGANVGGNS AGVFTDEPGK LTTDFFVNLV
DMSTKWQKAS TPGLYEGVDR DSGEVKWTAT PVDLIFGSNS ELRAIAEFYA MDDSKKKFVD
DFIAAWTKVM TADRFDV
//
