ID A0A0G3XE39_9SPHN Unreviewed; 537 AA.
AC A0A0G3XE39;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
GN ORFNames=AB433_07155 {ECO:0000313|EMBL:AKM09810.1}, GGR19_002053
GN {ECO:0000313|EMBL:MBB3990629.1};
OS Croceicoccus naphthovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM09810.1, ECO:0000313|Proteomes:UP000035287};
RN [1] {ECO:0000313|EMBL:AKM09810.1, ECO:0000313|Proteomes:UP000035287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM09810.1,
RC ECO:0000313|Proteomes:UP000035287};
RA Zeng Y., Huang Y.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3990629.1, ECO:0000313|Proteomes:UP000536420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102796 {ECO:0000313|EMBL:MBB3990629.1,
RC ECO:0000313|Proteomes:UP000536420};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
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}.
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; CP011770; AKM09810.1; -; Genomic_DNA.
DR EMBL; JACIEL010000011; MBB3990629.1; -; Genomic_DNA.
DR RefSeq; WP_047820495.1; NZ_JACIEL010000011.1.
DR AlphaFoldDB; A0A0G3XE39; -.
DR STRING; 1348774.AB433_07155; -.
DR KEGG; cna:AB433_07155; -.
DR PATRIC; fig|1348774.3.peg.1496; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000035287; Chromosome.
DR Proteomes; UP000536420; 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: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 ECO:0000313|EMBL:MBB3990629.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:MBB3990629.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035287}.
FT DOMAIN 11..397
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 492..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 130
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 537 AA; 60483 MW; 3F2194EA82482BDC CRC64;
MTDTPKCPYT TTDAGIRVQS DEHSLTVGRD GPIVLNDHYL IEQMANFNRE RIPERQPHAK
GSGAFGYYET TADVSKYTRA KIFQPGAKAE CAVRFSTVAG ERGSPDTWRD PRGFSVKIYT
EDGNFDMVGN NTPIFFIRDP LKFQHFIRSQ KRRADNGLRD HDMQWDFWTL SPESAHQVTY
LMGDRGIPKN WREMNGYSSH TYMLINEDGE KFWVKFHWHT DQGTESGNAH LTQDEADRMA
GIDGDFHRRD LFEAIAKGDH PSWTLKWQIM PFEEAKTYRI NPFDLTKVWP HDDYPLIEVG
KLTLTENPVD WDTQIEQLAF EPNNMVPGIG LSPDKMLLAR GFSYADAHRA RLGVNYKQIP
VNRAKNAEVH SYSRAGKGRT VNAVDPVYAP NSYGGPGAEP QVGGEATWMS DGDMVRAAYT
LREDDDDWSQ AGALVREVMD DEQRDRFVDN VAGHLADGVS EPILVRAFDY WRNVDKDIGD
RIERATRDLI GGKSEAPGMA SAKSIEGYSG IPSTSSLAKG EGQMGANQDL REPQSAK
//
