ID A0A432VFP9_9SPHN Unreviewed; 1119 AA.
AC A0A432VFP9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 12.
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 ECO:0000313|EMBL:RUN75623.1};
GN ORFNames=EJC47_15665 {ECO:0000313|EMBL:RUN75623.1};
OS Sphingomonas sp. TF3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2495580 {ECO:0000313|EMBL:RUN75623.1, ECO:0000313|Proteomes:UP000275325};
RN [1] {ECO:0000313|EMBL:RUN75623.1, ECO:0000313|Proteomes:UP000275325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF3 {ECO:0000313|EMBL:RUN75623.1,
RC ECO:0000313|Proteomes:UP000275325};
RA Afonin A., Vasilieva E., Akhtemova G., Zhukov V.;
RT "The Draft Genome Sequence of a Sphingomonas sp strain TF3.";
RL Submitted (DEC-2018) 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:RUN75623.1}.
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DR EMBL; RWKS01000018; RUN75623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432VFP9; -.
DR Proteomes; UP000275325; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.20.1530.20; -; 1.
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; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR016833; Put_Na-Bile_cotransptr.
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 Pfam; PF13593; SBF_like; 1.
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; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000275325};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 517..818
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 866..1119
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 484
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 652
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 480
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 611..637
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 483)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 1119 AA; 119899 MW; A66A85BA8EE1BABB CRC64;
MPTVRSLIAR SPIDPYLLLL IGTVGLAILL PARGSAQPLA ESAVTIAVGL LFFLYGARLS
PAAVWAGISH WRLQSLVFAS TFLIFPIIGL GASWAVRGLL PPDIGVGLLY LCLLPSTVQS
SIAFTAIARG NVPAALCSAS LSNLLGVVLT PVLVAVLLST AGGGFSITAI EGIAVQILLP
FVAGQAVRPW IGAWLLRHRT LTAVVDRGSI LLVVYAAFSA GVVAGVWTSL SVSDLVIVLA
IDLVILAIII GVTTLLSRRM GFSTEDEIAI VFCGSKKSMA GGIPMATILF AGHAVSLIVL
PLMLFHQAQL FVCATLARRY AKRPIEDAPP VAAQPSPVRI LTSASCHRAR VYISRPITLR
GLIHFSDQAR HAILCESQPE AALETAMNAE TKCPMGGGKV DGNAVLFEMT NRLWWPNQLD
LTVLHQNPPA GDPMDPDFDY AEAFKALDLA AVKADIFALM TESQDWWPAD FGHYGPLFIR
MAWHSAGTYR IGDGRGGAGS GQQRFAPLNS WPDNANLDKA RILLWPIKQK YGRALSWADL
LILTGNCALE SMGFKTAGFA GGRVDVWEPA TDVNWGAERE WLQTSDKPGG RYSGERELAD
PLAAVQMGLI YVNPEGPDGN PDPVLAAHDI RETFARMAMN DEETVALIAG GHTFGKTHGA
AVPDQYVGPE PEGAGIEQQG LGWANSYGTG NGADTITSGL EVTWTQQPTK WTNLFFDNLF
GHEWELTKSP AGAHQWVAKD AAEDVPDAHI PGKKHRPTML TTDLSLRFDP IYGPISKRFH
ENPDQFATAF AEAWYKLTHR DMGPHVRMLG AEVPAEPRIW QDPVPAPTHP LIDEADAAAL
KAQILDSGLS ISRLVKTAWA SASTFRGTDK RGGANGARIR LAPQKDWAVN EPVELAETLA
RLEAIQAGFN AGGKTVSLAD LIVLGGNAAV EAAAKKAGHD VSVPFTPGRT DASQEQTDAH
SFAPLEPKVD GFRNYVGGPS QYSAEELLVN RAQLLTLSAP EMTVLVGGLR VLGANFGGSS
HGVFTDRPET LTNDFFVNLL KTSTAMKWTA SEDGVFVARD RKTGAEQWAG TRVDLIFGSN
SQLRALAEAY ATDDAGAAFV RAFVAAWTKV MNLDRFDVA
//
