ID A0A172YS20_9GAMM Unreviewed; 505 AA.
AC A0A172YS20;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Catalase {ECO:0000313|EMBL:ANF83023.1};
GN ORFNames=A3K93_13060 {ECO:0000313|EMBL:ANF83023.1};
OS Acinetobacter sp. NCu2D-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1608473 {ECO:0000313|EMBL:ANF83023.1, ECO:0000313|Proteomes:UP000186584};
RN [1] {ECO:0000313|Proteomes:UP000186584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCu2D-2 {ECO:0000313|Proteomes:UP000186584};
RA Wilharm G.;
RT "Acinetobacter strain NCu2D-2 is the representative of a novel species.";
RL Submitted (APR-2016) 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 -!- 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}.
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; CP015594; ANF83023.1; -; Genomic_DNA.
DR RefSeq; WP_067731598.1; NZ_CP015594.1.
DR AlphaFoldDB; A0A172YS20; -.
DR STRING; 1608473.A3K93_13060; -.
DR KEGG; aciu:A3K93_13060; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000186584; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
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; 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; 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 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 Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..505
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008004973"
FT DOMAIN 24..406
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 381..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Basic and acidic 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; 56520 MW; 21E49CE7AC931730 CRC64;
MFKRSLLVAM LAAVTAGTQA APLTKDNGAP VGDNQNSITA GEHGGTLLQD VQLVQKLQRF
GRERIPERVV HARGVGAYGE FVATKDLSDL TLASLFKAGT KTPVFLRFST VIHGKGSPET
LRDPHGFAVK FYTQEGNWDL VGNQTPVFFI KDAIKFPDFI HAMKPSPINN VQDANRVFDF
LSSQPWATNM LTYVYGKQGV PTSFREQDGF GVHAYKLYND KGEYKYVKFN FRSKQGVKGL
NVKEAMEQQG KDFNHLTNDL YKNINAGNFP KWDLYIQVLD PKDLDSFDFD PLDPTKIWPT
DLVPEKKVGT LTLNRMPKNF FNETEQSAFA PGNLVPGIEP SEDRLLQGRI FSYSDTQMYR
LGANHQQIPV NRPIVAVNNN NQDGSMNVSE RDSDVNYEPS RIEPKPATEK ARAVQTPLMG
TVQQKGVKEQ NFKQAGELYR SYTAKEKDDL IMNLAADLGN VKDSETKHIM LSYFYKADAD
YGMRMTKAVN GNLATVKAKA AMLKD
//
