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Database: UniProt
Entry: N1UZH3_9MICC
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Original site: N1UZH3_9MICC 
ID   N1UZH3_9MICC            Unreviewed;       499 AA.
AC   N1UZH3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:EMY35781.1};
GN   ORFNames=D477_002546 {ECO:0000313|EMBL:EMY35781.1};
OS   Arthrobacter crystallopoietes BAB-32.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY35781.1, ECO:0000313|Proteomes:UP000010729};
RN   [1] {ECO:0000313|EMBL:EMY35781.1, ECO:0000313|Proteomes:UP000010729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-32 {ECO:0000313|EMBL:EMY35781.1,
RC   ECO:0000313|Proteomes:UP000010729};
RX   PubMed=23833141;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT   Revealing Genes for Bioremediation.";
RL   Genome Announc. 1:e00452-13(2013).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329}.
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:EMY35781.1}.
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DR   EMBL; ANPE02000062; EMY35781.1; -; Genomic_DNA.
DR   RefSeq; WP_005266948.1; NZ_ANPE02000062.1.
DR   AlphaFoldDB; N1UZH3; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000010729; Unassembled WGS sequence.
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; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF61; CATALASE; 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000010729}.
FT   DOMAIN          9..395
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         339
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   499 AA;  56597 MW;  CF835F8DB1509F57 CRC64;
     MADNTKPLTT VAGAPVADNQ DSLTAGPRGP MLLQDVWFLE KMAHFDREVI PERRMHAKGS
     GAFGTFTVTQ DITKYTSAKI FSEIGKKTEM FARFSTVAGE RGAADAERDI RGFALRFYTE
     EGNWDVVGNN TPVFFFRDPL KFPDLNHAVK RDPRTNLRSA ENNWDFWTNL PEALHQVTIV
     MSDRGIPASY RHMHGFGSHT FSFYNDAGER YWVKFHFRTQ QGIKNLTDEE AAKLVGDDRE
     SHQRDLFDSI EKGDFPKWTL FVQIMPEADA ETYKYHPFDL TKVWSKKDYP LIEVGEFELN
     RNPENYFADV EQAAFTPANV VPGISFSPDR MLQGRLFSYG DAARYRLGVN HHQIPVNYPR
     GAQLVNSFHR DGAMRVDGNQ GATPGINPNS YGRWQEQPAY REPQLGVGAV ADRFNYREDD
     ANYFEQPGIL FREKMTEEQR QVLFENTARA IDGASEATVE RHIANCTQAD PAYGEGVRKA
     IEALRAGKIS ETDVNSDSV
//
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