KATG_SYNE7
ID KATG_SYNE7 Reviewed; 720 AA.
AC Q31MN3; Q55110;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
GN OrderedLocusNames=Synpcc7942_1656;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15,
RP BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, AND SUBUNIT.
RX PubMed=8645214; DOI=10.1042/bj3160251;
RA Mutsuda M., Ishikawa T., Takeda T., Shigeoka S.;
RT "The catalase-peroxidase of Synechococcus PCC 7942: purification,
RT nucleotide sequence analysis and expression in Escherichia coli.";
RL Biochem. J. 316:251-257(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH HEME.
RA Wada K., Tada T.;
RT "Crystal structure of catalase-peroxidase from Synechococcus PCC 7942.";
RL Submitted (MAR-2004) to the PDB data bank.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01961};
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=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 mM for H(2)O(2) for catalase activity
CC {ECO:0000269|PubMed:8645214};
CC pH dependence:
CC Optimum pH is 6.5 for catalase activity. Active from pH 4.5 to 8.5.
CC {ECO:0000269|PubMed:8645214};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8645214, ECO:0000269|Ref.3}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09601.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D61378; BAA09601.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000100; ABB57686.1; -; Genomic_DNA.
DR PIR; S71130; S71130.
DR RefSeq; WP_011244741.1; NC_007604.1.
DR PDB; 1UB2; X-ray; 2.40 A; A=1-720.
DR PDB; 3WNU; X-ray; 2.20 A; A=1-720.
DR PDB; 3WXO; X-ray; 2.12 A; A=11-720.
DR PDB; 3X16; X-ray; 2.65 A; A=1-720.
DR PDB; 4PAE; X-ray; 3.21 A; A=1-720.
DR PDBsum; 1UB2; -.
DR PDBsum; 3WNU; -.
DR PDBsum; 3WXO; -.
DR PDBsum; 3X16; -.
DR PDBsum; 4PAE; -.
DR AlphaFoldDB; Q31MN3; -.
DR SMR; Q31MN3; -.
DR STRING; 1140.Synpcc7942_1656; -.
DR PeroxiBase; 2426; SeCP01_PCC7942.
DR PRIDE; Q31MN3; -.
DR EnsemblBacteria; ABB57686; ABB57686; Synpcc7942_1656.
DR KEGG; syf:Synpcc7942_1656; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_3; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1656-MON; -.
DR BRENDA; 1.11.1.21; 7781.
DR EvolutionaryTrace; Q31MN3; -.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8645214"
FT CHAIN 2..720
FT /note="Catalase-peroxidase"
FT /id="PRO_0000345095"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT BINDING 263
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT SITE 91
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 94..222
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 248)"
FT CROSSLNK 222..248
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 94)"
FT CONFLICT 56
FT /note="K -> Q (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="Missing (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="V -> F (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..329
FT /note="RML -> AVCS (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="S -> N (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="A -> P (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="A -> S (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="S -> T (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="A -> K (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="G -> V (in Ref. 1; BAA09601)"
FT /evidence="ECO:0000305"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:3WXO"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:3WXO"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4PAE"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3WXO"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:4PAE"
FT HELIX 373..380
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 395..411
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 445..454
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:3WXO"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 500..517
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 521..539
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 587..598
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 602..615
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 637..642
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 657..661
FT /evidence="ECO:0007829|PDB:3WXO"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:3WXO"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 673..676
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 682..692
FT /evidence="ECO:0007829|PDB:3WXO"
FT HELIX 694..696
FT /evidence="ECO:0007829|PDB:3WNU"
FT HELIX 697..712
FT /evidence="ECO:0007829|PDB:3WXO"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:3WXO"
FT TURN 717..719
FT /evidence="ECO:0007829|PDB:3X16"
SQ SEQUENCE 720 AA; 80078 MW; 93A4C2E9990F1A2F CRC64;
MTATQGKCPV MHGGATTVNI STAEWWPKAL NLDILSQHDR KTNPMGPDFN YQEEVKKLDV
AALKQDLQAL MTDSQDWWPA DWGHYGGLMI RLTWHAAGTY RIADGRGGAG TGNQRFAPLN
SWPDNTNLDK ARRLLWPIKQ KYGNKLSWAD LIAYAGTIAY ESMGLKTFGF AFGREDIWHP
EKDIYWGPEK EWVPPSTNPN SRYTGDRELE NPLAAVTMGL IYVNPEGVDG NPDPLKTAHD
VRVTFARMAM NDEETVALTA GGHTVGKCHG NGNAALLGPE PEGADVEDQG LGWINKTQSG
IGRNAVTSGL EGAWTPHPTQ WDNGYFRMLL NYDWELKKSP AGAWQWEPIN PREEDLPVDV
EDPSIRRNLV MTDADMAMKM DPEYRKISER FYQDPAYFAD VFARAWFKLT HRDMGPKARY
IGPDVPQEDL IWQDPIPAGN RNYDVQAVKD RIAASGLSIS ELVSTAWDSA RTYRNSDKRG
GANGARIRLA PQKDWEGNEP DRLAKVLAVL EGIAAATGAS VADVIVLAGN VGVEQAARAA
GVEIVLPFAP GRGDATAEQT DTESFAVLEP IHDGYRNWLK QDYAATPEEL LLDRTQLLGL
TAPEMTVLIG GLRVLGTNHG GTKHGVFTDR EGVLTNDFFV NLTDMNYLWK PAGKNLYEIC
DRKTNQVKWT ATRVDLVFGS NSILRAYSEL YAQDDNKEKF VRDFVAAWTK VMNADRFDLD
