ID K9HM57_9PROT Unreviewed; 504 AA.
AC K9HM57;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Catalase {ECO:0000313|EMBL:EKV31433.1};
GN ORFNames=C882_3806 {ECO:0000313|EMBL:EKV31433.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV31433.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV31433.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV31433.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(2013).
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|ARBA:ARBA00000720};
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:EKV31433.1}.
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DR EMBL; ANHY01000006; EKV31433.1; -; Genomic_DNA.
DR RefSeq; WP_009539914.1; NZ_ANHY01000006.1.
DR AlphaFoldDB; K9HM57; -.
DR STRING; 1238182.C882_3806; -.
DR PATRIC; fig|1238182.3.peg.1469; -.
DR eggNOG; COG0753; Bacteria.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000009881; 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; 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; 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: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; 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:UP000009881}.
FT DOMAIN 8..393
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 338
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 504 AA; 57772 MW; 66DB48E16D7D4ED4 CRC64;
MAERPKLTTT AGAPVGDNQH ALTAGPRGPL LLQDYQLVEK LAHQNRERIP ERVVHAKGWG
AFGTFTVTND ISKYTNARIF SEVGKKTDLL ARFSTVAGEQ GAADAERDVR GFSVKFYTEE
GNWDLVGNNT PIFFVRDPYK FPDFIRTQKR HPRTNLRSPT AQWDFWSLCP ESIHQITILM
SDRGLPQGPQ YMNGYGSHTF SFWNDAGERY WVKFHFKTRQ GHKHYTNAEA QDLIGKTRES
YQEELYGAID RGDYPKWTLY VQVMPEEEAE NTPYNPFDLT KVWPHKDYPL IEVGEMELNR
NPDNYFAEIE QAAFSPSNVV RGISFSPDKM LQARIFSYAD AHRYRLGGHY EALPVNQPKC
PVAHYHKDGL LRFFADNNPP DAYYEPNSFG GPAEDPKYLE PPLRISGDAR RYVQHELEDD
FSQARALFEM FDDGQKQRLF NNVAEAIHGV PEEIFERQMN HFEAVSPDYA KGVRAAVEAL
PAKDEKMKTQ MDMDRMAVHP KQGG
//
