ID A0A1M7GH46_9GAMM Unreviewed; 478 AA.
AC A0A1M7GH46;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
GN ORFNames=SAMN05428972_2604 {ECO:0000313|EMBL:SHM15448.1};
OS Rhodanobacter sp. OK091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1881037 {ECO:0000313|EMBL:SHM15448.1, ECO:0000313|Proteomes:UP000184078};
RN [1] {ECO:0000313|EMBL:SHM15448.1, ECO:0000313|Proteomes:UP000184078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK091 {ECO:0000313|EMBL:SHM15448.1,
RC ECO:0000313|Proteomes:UP000184078};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRCH01000002; SHM15448.1; -; Genomic_DNA.
DR RefSeq; WP_072761253.1; NZ_FRCH01000002.1.
DR AlphaFoldDB; A0A1M7GH46; -.
DR STRING; 1881037.SAMN05428972_2604; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000184078; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184078}.
FT DOMAIN 9..392
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
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 478 AA; 54576 MW; 6046798548743801 CRC64;
MNTKLATLTT SSGAPVPDNQ NSLTAGPRGP LLVQDHQLFE KHAHFNRERI PERVVHAKGS
AAHGTLTITH DITKYSRAKV FKPGSETPLF LRFSTVAGER GAADAERDVR GFAIKFYTEE
GNWDLVGNNT PVFFVRDPYK FPDFIHTQKR DPRTNMRSAT AMWDFWSLSP ESLHQVTTLM
SDRGLPASLR HMHGFGSHTY SFWNDQDERY WVKFHFKTQQ GIENWTNEHA AKVIGDDRES
HQRDLYEAIE RKDFPKWTMY IQIMPEKDAE KTPYNPFDLT KVWPHKDYPL IEVGVMELNK
NPENYHAEVE QSSFSPANVV PGISHSPDKM LQFRIFSYAD AARYRLGTNH EALEVNRPRC
PVHNYYRDGE MRFDVNGGGS VNYEPNSFNG PVEDKSTKEP PLKISGDADR YDHRQGNDDY
TQPGDLFRLM NADQQQQLFN NIAAAMQGVP EEIIRRQLGH FSKADPAYGA GVAKALSL
//
