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Database: UniProt
Entry: F5ZDE9_ALTNA
LinkDB: F5ZDE9_ALTNA
Original site: F5ZDE9_ALTNA 
ID   F5ZDE9_ALTNA            Unreviewed;       689 AA.
AC   F5ZDE9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 69.
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   OrderedLocusNames=ambt_11955 {ECO:0000313|EMBL:AEF03911.1};
OS   Alteromonas naphthalenivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF03911.1, ECO:0000313|Proteomes:UP000000683};
RN   [1] {ECO:0000313|EMBL:AEF03911.1, ECO:0000313|Proteomes:UP000000683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC   {ECO:0000313|Proteomes:UP000000683};
RX   PubMed=21705606; DOI=10.1128/JB.05252-11;
RA   Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA   Oh T.K., Kim J.F.;
RT   "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT   bacterium Alteromonas sp. strain SN2.";
RL   J. Bacteriol. 193:4292-4293(2011).
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}.
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DR   EMBL; CP002339; AEF03911.1; -; Genomic_DNA.
DR   RefSeq; WP_013784842.1; NC_015554.1.
DR   AlphaFoldDB; F5ZDE9; -.
DR   KEGG; alt:ambt_11955; -.
DR   eggNOG; COG0693; Bacteria.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_3_0_6; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000000683; Chromosome.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}.
FT   DOMAIN          29..417
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   BINDING         73
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         113
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         162
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         359
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         363
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         370
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ   SEQUENCE   689 AA;  77263 MW;  A3C2317B3C6120E5 CRC64;
     MAESFKYQGQ KGQGGELHQT AGNGHPAMTT AQGCPIHDDQ NSLKAGQRGP TVLEDHVLRE
     KIFHFDHERI PERVVHARGF GAHGYFETYE SLSDITSADI FQRKGEKTPV FTRFSTVAGN
     KGSPDLARDV RGFAVKFYTQ QGNWDLVGNN IPVFFIQDAI KFPDLIHSAK QEPDRGFPQA
     QTAHDNFWDF TSLSPESTHM LMWAMSDRAI PRSFRFMEGF GVHTFKFINA EGEMKYVKFH
     WKPKQGLQSV VWNEALKING ADPDFHRRDM WNALQAGDFP EWELGVQVFD QDFADNFEFD
     VLDATKLIPE EQVPVKIVGK MVLNNVVDNF FAETEQVAFC TQNIVPGIDF TNDPLLQGRN
     FSYLDTQLKR LGSTNFTQLP INAPKCPMRH FQQDGHMAMQ NPKGRANYEP NSWDADENNP
     RACPETGYQS HAEPMEGSKT RYRSETFADH YSQARQFYIS QTETEQKHMR DAFAFELSKV
     ERLAIRERVV SHLLNVDKTL AESVAQELGF LEMPEPAEAA MPTRQDLPVS DALSILKNAP
     NTFKGRKLGI LVSDGIDADM LSNVIDSLMA EGAMFELVAP KVGGVTCSKG KHIAAHQKVD
     GGPSVLYDAV LLLLSEDGAT SLSMKPEAKD FVSDAHAHQK FVGYTANAMP LIKAAGLGDA
     MDDGWLDIES IKPDAFIKQL RDIRFWARG
//
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