ID N9CED1_9GAMM Unreviewed; 505 AA.
AC N9CED1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=F941_00098 {ECO:0000313|EMBL:ENV84182.1};
OS Acinetobacter bouvetii DSM 14964 = CIP 107468.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120925 {ECO:0000313|EMBL:ENV84182.1, ECO:0000313|Proteomes:UP000018460};
RN [1] {ECO:0000313|EMBL:ENV84182.1, ECO:0000313|Proteomes:UP000018460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107468 {ECO:0000313|EMBL:ENV84182.1,
RC ECO:0000313|Proteomes:UP000018460};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter bouvetii CIP 107468.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
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|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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:ENV84182.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APQD01000002; ENV84182.1; -; Genomic_DNA.
DR RefSeq; WP_005006634.1; NZ_KB892275.1.
DR AlphaFoldDB; N9CED1; -.
DR PATRIC; fig|1120925.3.peg.112; -.
DR eggNOG; COG0753; Bacteria.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000018460; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF23; CATALASE-2; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 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|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|RuleBase:RU000498};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..505
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004140982"
FT DOMAIN 24..406
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 353
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:PIRSR038928-2"
SQ SEQUENCE 505 AA; 56546 MW; 34069E58CDDBF766 CRC64;
MFKRSLLVAM FTSATAAAQA APLTKDNGAP VGDNQNSITA GPQGGTMLQD VQLVQKLQRF
GRERIPERVV HARGTGAYGE FVATKDLSDI TLASLFKAGT KTPVFLRFST VIHGKGSPET
LRDPHGFAIK FYTQEGNWDL VGNQTPVFFI RDAIKFPDFI HAMKPSPINN VQDANRVFDF
LSSQPWATNM LTYVYGKQGV PTSYREQDGF GVHAYKLYNG KGEFKYVKFN FRSQQGVKGL
NVKEAAEQQA KDFNHLTNDL YANINKGNFP KWDLYVQILD PEDFVKFDFD PLDPTKIWPT
DIVPETKAGT LTLNRMPKNF FNETEQSAFA PGNLVPGIEP SEDRLLQGRI FSYSDTQMYR
LGANHQQIPV NRPVVAVSNN NQDGYMNVSE RDSDVNYEPS RKEPKAATEK ARAVQTPLTG
TVQQIGTKER NFKQAGELYR SYTAKERDDL IMNLAADLGN VKDSETKHIM LSYFYKADAD
YGMRMTEAVK GDMATVKAKA AKLKD
//