ID A0A1V0AGN9_9ACTN Unreviewed; 552 AA.
AC A0A1V0AGN9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Catalase {ECO:0000313|EMBL:AQZ69252.1};
GN ORFNames=BKM31_54275 {ECO:0000313|EMBL:AQZ69252.1};
OS Nonomuraea sp. ATCC 55076.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ69252.1, ECO:0000313|Proteomes:UP000190797};
RN [1] {ECO:0000313|Proteomes:UP000190797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX PubMed=28626548; DOI=10.1039/c6md00637j;
RA Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA Seyedsayamdost M.R.;
RT "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT date and the kistamicin biosynthetic gene cluster.";
RL Med. Chem. Commun. 8:780-788(2017).
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}.
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DR EMBL; CP017717; AQZ69252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0AGN9; -.
DR STRING; 1909395.BKM31_54275; -.
DR KEGG; noa:BKM31_54275; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000190797; 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 Reference proteome {ECO:0000313|Proteomes:UP000190797}.
FT DOMAIN 19..411
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 354
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 552 AA; 63082 MW; 02FBF0A9BB6677E3 CRC64;
MTDVSGMGSR PDDERPVLTN RQGHPVYDNQ NQRTVGPRGP ATLENYQFLE KISHFDRERI
PERVVHARGA LSYGYFEAYG TFGDEPISRY TRAKLFQERG KRTDIALRFS TVIGGRDSAE
TARDPRGFAI KFYTEDGNWD LVGNNLAVFF IRDAIKFPDV IHALKPDPVT FRQDPNRIFD
FMSQTPESMH MLVNLFSPRG IPADYRHMQG FGVNTYKWVN AQGETHLVKY HWMPKQGVRS
MTEADAAAVQ AHDLGHATKD LYEAIERGDY PEWELLVQIM TDDEHPELDF DPLDDTKVWP
ENDFPPQAVG RIVLNRNVEN QFAENEQSAF GTGVLVDGLD FSDDKMLIGR TFSYSDTQRY
RVGPNYLQLP VNQTKAACRT NQRDGQMAYF VDTGGENPHV NYEPSIRGGL REAEYAHPDE
VGPTITGRLT RKRIPRTNDY KQAGQRYLLM DDWERDDLVR NFVANLKQCD RAIQERMVWH
FLLVEDDLGL RVGEGLGITP DDVAGLEPLR SQDLTEEDRD RLAKLGRNGP RDVEGLKMTH
CVPNERAVHA EQ
//
