ID A0A0S1B3W5_9GAMM Unreviewed; 368 AA.
AC A0A0S1B3W5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN Name=katA_2 {ECO:0000313|EMBL:ALJ29670.1};
GN ORFNames=AOT14_33300 {ECO:0000313|EMBL:ALJ29670.1};
OS Stenotrophomonas acidaminiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=128780 {ECO:0000313|EMBL:ALJ29670.1, ECO:0000313|Proteomes:UP000061010};
RN [1] {ECO:0000313|EMBL:ALJ29670.1, ECO:0000313|Proteomes:UP000061010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZAC14D2_NAIMI4_2 {ECO:0000313|EMBL:ALJ29670.1,
RC ECO:0000313|Proteomes:UP000061010};
RX PubMed=26659678;
RA Vinuesa P., Ochoa-Sanchez L.E.;
RT "Complete Genome Sequencing of Stenotrophomonas acidaminiphila
RT ZAC14D2_NAIMI4_2, a Multidrug-Resistant Strain Isolated from Sediments of a
RT Polluted River in Mexico, Uncovers New Antibiotic Resistance Genes and a
RT Novel Class-II Lasso Peptide Biosynthesis Gene Cluster.";
RL Genome Announc. 3:e01433-15(2015).
CC -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity.
CC {ECO:0000256|PIRNR:PIRNR000296}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRNR:PIRNR000296};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|PIRNR:PIRNR000296}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012900; ALJ29670.1; -; Genomic_DNA.
DR RefSeq; WP_054667952.1; NZ_CP012900.1.
DR AlphaFoldDB; A0A0S1B3W5; -.
DR KEGG; sacz:AOT14_33300; -.
DR PATRIC; fig|128780.6.peg.3367; -.
DR OrthoDB; 255727at2; -.
DR Proteomes; UP000061010; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08153; srpA_like; 1.
DR Gene3D; 1.20.1280.120; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR024168; Catalase_SrpA-type_pred.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; CATALASE; 1.
DR Pfam; PF00199; Catalase; 1.
DR PIRSF; PIRSF000296; SrpA; 1.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW Iron {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000296,
KW ECO:0000256|PIRSR:PIRSR000296-2};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000296};
KW Peroxidase {ECO:0000256|PIRNR:PIRNR000296};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..367
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 348..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
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:PIRSR000296-2"
SQ SEQUENCE 368 AA; 40073 MW; 2115014EFFF7E762 CRC64;
MPLFPYTRAG RPPPAPRRHT PLPWIALIAL ILGAIALAFA WLAGWIGRER LTAQRFTDTI
EATGAAHPGF RRAHSKGVCV SGWFEPSAQA PSLSRARVFA QPRVPVLGRL SIGGGDPHGA
DGNARVRSIA LQLVGDDGQE WRMAMNSFPF FAVPTPEAFF EQTRAQVPDP ATGKPDPAKM
AAVLAKYPSA QAFQQWARTA PWTDSWANTT FNGINSFWFT NAQGQKRAVR WRWQPQAAVV
ELDAAARGRA DADFLSQDLQ RRLAAGPLRW NLVVSLAGPG DAIDDPSVPW PASRPEVMAG
VLSLDRMQSQ EQGACGELNF DPLILPDGMR GSDDPVLAAR SAIYSQSFNR RERERAAGAP
AQPQEATR
//
