ID A0A2C8Y7K1_9MICO Unreviewed; 482 AA.
AC A0A2C8Y7K1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Catalase {ECO:0000313|EMBL:SOE46161.1};
GN ORFNames=SAMN06296378_0128 {ECO:0000313|EMBL:SOE46161.1};
OS Salinibacterium xinjiangense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Salinibacterium.
OX NCBI_TaxID=386302 {ECO:0000313|EMBL:SOE46161.1, ECO:0000313|Proteomes:UP000219440};
RN [1] {ECO:0000313|EMBL:SOE46161.1, ECO:0000313|Proteomes:UP000219440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.05381 {ECO:0000313|EMBL:SOE46161.1,
RC ECO:0000313|Proteomes:UP000219440};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; OCST01000001; SOE46161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C8Y7K1; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000219440; 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 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; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; 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:UP000219440}.
FT DOMAIN 7..391
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 COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 336
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 482 AA; 54211 MW; F0DE2E558D07C8FB CRC64;
MTDNFTTSQS GAPLASDEHS LTAGPDGSTV LHDRFLVEKL AAFNRERVPE RNPHAKGGGA
FGEFQVTEDV SQYTRAAVFQ PGAKSEILLR FSSVAGEQGS PDTWRDVRGY SLRFYTTEGN
YDVVGNNTPV FFIRDAMKFP DFIHSQKRLG GSGLRDADMQ WDFWTLSPES SHQVTYLMGD
RGLSKSWRHL NGYGSHTYQW INAAGERHWI QYHFKSRQGV ERMSAEEGEK LAGSDADYYR
RDLYNAIETG DFPIWDVFVQ VMPYEDAKTY RFNPFDITKT WSHADYPLVK VGEYTLNRNP
QNFFAEIEQA AFSPANLVPG IDISPDKMLM ARVHSYPDAQ RYRIGTNYNE LPVNKPHAAP
VANYQHEGSM RYEFSDATAR TYTPNSYGGP VADPARAGEG SWESDGTLTR AAATLHSEDD
DFGQAGTLYR DIFDEGSKAR LLETLTGQGK GITVPEIRER FFWYWSNVDA TLGASLRETV
GA
//
