CATA_HAEIN
ID CATA_HAEIN Reviewed; 508 AA.
AC P44390;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; Synonyms=hktE; OrderedLocusNames=HI_0928;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=8188593; DOI=10.1128/jb.176.10.2914-2921.1994;
RA Bishai W.R., Smith H.O., Barcak G.J.;
RT "A peroxide/ascorbate-inducible catalase from Haemophilus influenzae is
RT homologous to the Escherichia coli katE gene product.";
RL J. Bacteriol. 176:2914-2921(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
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:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By hydrogen peroxide.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; U02682; AAA20441.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22587.1; -; Genomic_DNA.
DR PIR; D64103; D64103.
DR RefSeq; NP_439088.1; NC_000907.1.
DR RefSeq; WP_005693274.1; NC_000907.1.
DR AlphaFoldDB; P44390; -.
DR SMR; P44390; -.
DR STRING; 71421.HI_0928; -.
DR PRIDE; P44390; -.
DR EnsemblBacteria; AAC22587; AAC22587; HI_0928.
DR KEGG; hin:HI_0928; -.
DR PATRIC; fig|71421.8.peg.969; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_6; -.
DR OMA; WTCYVQV; -.
DR PhylomeDB; P44390; -.
DR BioCyc; HINF71421:G1GJ1-968-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR CDD; cd08156; catalase_clade_3; 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; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; PTHR11465; 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; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..508
FT /note="Catalase"
FT /id="PRO_0000084986"
FT ACT_SITE 63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 346
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:0000250"
FT CONFLICT 357
FT /note="N -> C (in Ref. 1; AAA20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="N -> T (in Ref. 1; AAA20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="N -> S (in Ref. 1; AAA20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="N -> T (in Ref. 1; AAA20441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 57680 MW; 4FAFC16DB44043B0 CRC64;
MSSQCPFSHL AATNLTMGNG APVADNQNSL TAGPRGPLLA QDLWLNEKLA DFVREVIPER
RMHAKGSGAF GTFTVTHDIT KYTRAKIFSE VGKKTEMFAR FTTVAGERGA ADAERDIRGF
ALKFYTEEGN WDLVGNNTPV FFLRDPRKFP DLNKAVKRDP RTNMRSATNN WDFWTLLPEA
LHQVTVVMSD RGIPASYRHM HGFGSHTYSF WNEAGERFWV KFHFRTQQGI KNLTDAEAAE
IIANDRESHQ RDLYEAIERG DFPKWTLFVQ IMPEADAEKV PYHPFDLTKV WSKKDYPLIE
VGEFELNRNP ENFFADVEQS AFAPSNLVPG IGASPDRMLQ ARLFNYADAQ RYRLGVNYRQ
IPVNRPRCPV HSNQRDGQGR VDGNYGSLPH YEPNSFSQWQ QQPDFAEPPL RINGDAAHWD
YRNDDNDYFS QPRALFNLMN AEQKQSLFNN TAAAMGDAPD FIKYRHIRNC HWCDAAYGEG
VAKALGLTVE DALKARDTDP ALGQGGLL
