ID A0A1S9ZHK8_9GAMM Unreviewed; 506 AA.
AC A0A1S9ZHK8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
GN ORFNames=B0180_09075 {ECO:0000313|EMBL:OOR83009.1};
OS Moraxella canis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=90239 {ECO:0000313|EMBL:OOR83009.1, ECO:0000313|Proteomes:UP000190322};
RN [1] {ECO:0000313|EMBL:OOR83009.1, ECO:0000313|Proteomes:UP000190322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 8415A {ECO:0000313|EMBL:OOR83009.1,
RC ECO:0000313|Proteomes:UP000190322};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Moore E.;
RT "Draft genome sequence of Moraxella canis CCUG 8415A type strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OOR83009.1}.
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DR EMBL; MUXT01000009; OOR83009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9ZHK8; -.
DR Proteomes; UP000190322; 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; 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}.
FT DOMAIN 14..398
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 344
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 506 AA; 57946 MW; EC0061698FCE460D CRC64;
MSEKKCPYDH TYLTMSNGAP VPSNQDSMSA GPRGPLLMQD LWLNEKLGDF AREVIPERRM
HAKGSGAFGT FTVTNDITQY TKAKMFSEVG KKTEMFARFT TVAGERGAAD AERDIRGFAL
KFYTEEGNWD MVGNNTPVFF IRDPKKFPDL NKAVKRDPKT NLRSPTNNWD WWTLLPEAFH
QVTIVMSDRG IPKSYRHMHG FSSHTYSFIN AENERFWVKM HFRTQQGIEN LTDAEAEAVI
AKDRESNQRD LFNAIEEGNF PKWKMYVQIM PETEAETVPY HPFDLTKVWP KGDYPLIEVG
EFELNKNPEN FFLDVEQSAF APSNLVPGIS VSPDRMLQAR LVNYADAQRY RLGVNRNQIP
VNAPRCPVYS NHRDGLGRVG DNYGGRPHYE PNSFGQWQDQ PHLAEPPLKI SGDAKIWDFR
QDDEDYFSQP RALFNLMNDE QKQALFGNTA RNMDDAPDFI KYRHIRNCNK CHPEYAAGVA
KALGLTVEDA EKARESDPAR HLPSLL
//
