ID N9T0L7_9GAMM Unreviewed; 507 AA.
AC N9T0L7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=F902_01154 {ECO:0000313|EMBL:ENX60606.1};
OS Acinetobacter higginsii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70347 {ECO:0000313|EMBL:ENX60606.1, ECO:0000313|Proteomes:UP000013084};
RN [1] {ECO:0000313|EMBL:ENX60606.1, ECO:0000313|Proteomes:UP000013084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 70.18 {ECO:0000313|EMBL:ENX60606.1,
RC ECO:0000313|Proteomes:UP000013084};
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 sp. CIP 70.18.";
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:ENX60606.1}.
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DR EMBL; APRN01000033; ENX60606.1; -; Genomic_DNA.
DR RefSeq; WP_005201668.1; NZ_KB850071.1.
DR AlphaFoldDB; N9T0L7; -.
DR PATRIC; fig|1217700.3.peg.1107; -.
DR HOGENOM; CLU_010645_4_0_6; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000013084; 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..507
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004152574"
FT DOMAIN 24..406
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
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 507 AA; 57173 MW; 79769C133B5F02AD CRC64;
MFKRTFLFTI MAATLGTAYA APLTKDNGAP VGDNQNSMTA GANGATLLQD VQLIQKLQRF
GRERIPERVV HARGTGVYGD FVASKDLSDL TVASMFKAGT TTPVFVRFST VIHPKGSPET
ARDPHGFAVK FYTQQGNWDL VGNNLPVFFI RDAIKFPDFV HAMKPDPVTN VQDPNRIFDF
LKSQPWSINM LTYVYSNLGT PESYRTLDGF GVHAFKLYND KGEYKYVKFN WRSKQGVKGL
NLDQVREVQG RDWNHLTNDM YKNVYAGNYP KWDLYIQVLD PKDLDKFDFN PLDATKIWPT
DLLPEVKVGT LTLNRMPKNF FQETEQSAFA PGNLIPGIEP SEDRLLQGRI FSYSDTQLYR
LGANHQQIPV NRPRVAVNNN NQEGFMNMGQ TESQVNYEPS TIEPKLSTEI ARAVQTPLQG
TVLQQAIQKQ QPFKQAGELY RSYSALEKND LIRNLAADLG QVKDIETKTI MVSYFYKADA
DYGTRLAKAV GVNLKNAQAK AAQLKDE
//
