ID H2CBZ8_9LEPT Unreviewed; 481 AA.
AC H2CBZ8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Catalase related subgroup domain-containing protein {ECO:0000313|EMBL:EHQ08670.1};
GN ORFNames=Lepil_4022 {ECO:0000313|EMBL:EHQ08670.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ08670.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ08670.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ08670.1,
RC ECO:0000313|Proteomes:UP000005737};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; JH597773; EHQ08670.1; -; Genomic_DNA.
DR RefSeq; WP_002775558.1; NZ_JH597773.1.
DR AlphaFoldDB; H2CBZ8; -.
DR STRING; 183.GCA_002009735_00244; -.
DR HOGENOM; CLU_010645_2_0_12; -.
DR Proteomes; UP000005737; 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:UP000005737}.
FT DOMAIN 10..396
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 340
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 481 AA; 54459 MW; 837B230DB5421F09 CRC64;
MSEQKCPFHT TTAGAPIADN QNSKTAGPRG PVLLEDWQLL EKLAHQNRER IPERVVHAKG
WGAFGTLTIT KDISRYSKAK VFSGIGKKTP MLARFSTVAG EMGAADAERD VRGFALKFYT
EEGNWDMVGN NTPVFFIRDP LKFPDFIHTQ KRHPKTNLRS NTAAWDFWSL SPESLHQITI
LMSDRGIPVS PRFMNGYGSH TYSFWNEKGE RYWVKFHFKT QQGHKTLTNA EAEAVVAKSR
ETYQEDLFYS IEKGEFPKWT MYVQVMPEAD AEKTSYNPFD LTKVWPHKDY PLIEVGVMEL
NRNPDNYFAE IEQAAFSPSN VVPGIGFSPD KMLQARIFSY ADAHRYRLGT HYEALPVNAP
KCPVHHYHKD GSMNFIGQKT GNVDAYYEPN SFGGAVATGD TSEPALRISG DGDRYDHREG
NDDYSQARVL FEMFDAGQKE RLFSNIAASM KGVPDFIVKR QLVHFEKVHP DYAAGVKKAL
A
//
