ID M7NVP8_9BACL Unreviewed; 681 AA.
AC M7NVP8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN Name=katE_2 {ECO:0000313|EMBL:EMR05725.1};
GN ORFNames=C772_02213 {ECO:0000313|EMBL:EMR05725.1};
OS Bhargavaea cecembensis DSE10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR05725.1, ECO:0000313|Proteomes:UP000011919};
RN [1] {ECO:0000313|EMBL:EMR05725.1, ECO:0000313|Proteomes:UP000011919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE10 {ECO:0000313|EMBL:EMR05725.1,
RC ECO:0000313|Proteomes:UP000011919};
RX PubMed=23766406;
RA Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT Chagos-Laccadive Ridge System in the Indian Ocean.";
RL Genome Announc. 1:e00346-13(2013).
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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=1.11.1.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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:EMR05725.1}.
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DR EMBL; AOFT01000011; EMR05725.1; -; Genomic_DNA.
DR RefSeq; WP_008299966.1; NZ_AOFT01000011.1.
DR AlphaFoldDB; M7NVP8; -.
DR STRING; 1235279.C772_02213; -.
DR PATRIC; fig|1235279.3.peg.2219; -.
DR eggNOG; COG0693; Bacteria.
DR eggNOG; COG0753; Bacteria.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000011919; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000011919}.
FT DOMAIN 28..416
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 511..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 148
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 72
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 112
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 161
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 358
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 362
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-2"
FT BINDING 369
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 681 AA; 76898 MW; FCE767030DE63402 CRC64;
MDKRQDEKNS KDEQLKAFRV DDKGKALTTN QGLKMSEDEF SLKAGVRGPT IMEDFHFREK
LTHFDHERIP ERVVHARGFA VHGEFQLYKN MKKYTSAKFL QDTSKKTPVF VRFSTVNGSR
GSADTARDAR GFATKFYTEE GNYDLVANNI PVFFIQDAIK FPDVVHSFKP EPDNDIPQAS
TAHDTFWDFV ANNQESAHMI MWIMSDRAIP RSFRMMEGFG VHAFRFVNDE GKAHFVKFHW
KPVLGTHSLV WDEAHKLMGI DPDFHRNDIW NAVEQGFYPE YELGVQILAE EDEFSLGFDI
LDSTKIWPEE DIPVNIIGKM TLNRNVDNFF AETEQVAFHV GNVVPGIDFT NDPLLQGRLF
SYTDTQLIRL GGPNFHEIPI NRPVVQFHNN QREGYHRQTI NLGKVSYHRN SLAGNTPAPV
PPEKGGYATY QEKVEGRKVR ARSESFEDHF SQATLFWNSM TNHEKAHIIE AFSFELGKVK
SQSVRQQVVD MFANVSVELA TAFAVNIGAA PPEEGGSGVT KSSPALSQEN TPKSAETRRV
AVILTDGFNG PEVNDVLEKL MTSGVVPEII SERIGTVRGT DGVQLKAQHT FLTAKSVMFD
AVYMIRGSRQ NKKFNKDAAY FIDEAFSHYK PIGATGEGIS WLKVNHLEGK PGVISGTDIG
AFTEEFVKAI AAHRFWERVL V
//
