KATG_BURP1
ID KATG_BURP1 Reviewed; 728 AA.
AC Q3JNW6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=BURPS1710b_3366;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
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}.
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DR EMBL; CP000124; ABA50840.1; -; Genomic_DNA.
DR RefSeq; WP_004522123.1; NC_007434.1.
DR PDB; 5KQ0; X-ray; 1.80 A; A/B=1-728.
DR PDB; 5KQ2; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5KQ3; X-ray; 1.85 A; A/B=1-728.
DR PDB; 5KQ6; X-ray; 1.62 A; A/B=1-728.
DR PDB; 5KQH; X-ray; 1.82 A; A/B=1-728.
DR PDB; 5KQI; X-ray; 1.87 A; A/B=1-728.
DR PDB; 5KQK; X-ray; 1.75 A; A/B=1-728.
DR PDB; 5KQN; X-ray; 1.75 A; A/B=1-728.
DR PDB; 5KQQ; X-ray; 1.87 A; A/B=1-728.
DR PDB; 5KSF; X-ray; 1.75 A; A/B=1-728.
DR PDB; 5KSG; X-ray; 1.62 A; A/B=1-728.
DR PDB; 5KSK; X-ray; 1.69 A; A/B=1-728.
DR PDB; 5KSN; X-ray; 1.87 A; A/B=1-728.
DR PDB; 5KT8; X-ray; 2.00 A; A/B=1-728.
DR PDB; 5KT9; X-ray; 1.88 A; A/B=1-728.
DR PDB; 5L02; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5L05; X-ray; 1.70 A; A/B=1-728.
DR PDB; 5SW4; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5SW5; X-ray; 2.05 A; A/B=1-728.
DR PDB; 5SW6; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5SX0; X-ray; 2.00 A; A/B=1-728.
DR PDB; 5SX1; X-ray; 1.80 A; A/B=1-728.
DR PDB; 5SX2; X-ray; 2.15 A; A/B=1-728.
DR PDB; 5SX3; X-ray; 2.00 A; A/B=1-728.
DR PDB; 5SX6; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5SX7; X-ray; 1.95 A; A/B=1-728.
DR PDB; 5SXQ; X-ray; 2.10 A; A/B=1-728.
DR PDB; 5SXR; X-ray; 1.69 A; A/B=1-728.
DR PDB; 5SXS; X-ray; 1.89 A; A/B=1-728.
DR PDB; 5SXT; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5SXW; X-ray; 1.60 A; A/B=1-728.
DR PDB; 5SXX; X-ray; 1.70 A; A/B=1-728.
DR PDB; 5SYH; X-ray; 1.65 A; A/B=1-728.
DR PDB; 5SYI; X-ray; 1.70 A; A/B=1-728.
DR PDB; 5SYJ; X-ray; 1.88 A; A/B=1-728.
DR PDB; 5SYK; X-ray; 1.80 A; A/B=1-728.
DR PDB; 5SYL; X-ray; 1.95 A; A/B=1-728.
DR PDB; 5SYU; X-ray; 1.80 A; A/B=1-728.
DR PDB; 5SYV; X-ray; 1.75 A; A/B=1-728.
DR PDB; 5SYW; X-ray; 1.85 A; A/B=1-728.
DR PDB; 5SYY; X-ray; 1.85 A; A/B=1-728.
DR PDB; 5TXQ; X-ray; 1.90 A; A/B=1-728.
DR PDB; 5V4O; X-ray; 1.95 A; A/B=1-728.
DR PDB; 5V53; X-ray; 1.70 A; A/B=1-728.
DR PDB; 6B9B; X-ray; 1.80 A; A/B=1-728.
DR PDB; 6CAW; X-ray; 1.95 A; A/B=1-728.
DR PDB; 6CC6; X-ray; 1.80 A; A/B=1-728.
DR PDB; 6CDQ; X-ray; 1.92 A; A/B=1-728.
DR PDB; 6CEK; X-ray; 1.80 A; A/B=1-728.
DR PDBsum; 5KQ0; -.
DR PDBsum; 5KQ2; -.
DR PDBsum; 5KQ3; -.
DR PDBsum; 5KQ6; -.
DR PDBsum; 5KQH; -.
DR PDBsum; 5KQI; -.
DR PDBsum; 5KQK; -.
DR PDBsum; 5KQN; -.
DR PDBsum; 5KQQ; -.
DR PDBsum; 5KSF; -.
DR PDBsum; 5KSG; -.
DR PDBsum; 5KSK; -.
DR PDBsum; 5KSN; -.
DR PDBsum; 5KT8; -.
DR PDBsum; 5KT9; -.
DR PDBsum; 5L02; -.
DR PDBsum; 5L05; -.
DR PDBsum; 5SW4; -.
DR PDBsum; 5SW5; -.
DR PDBsum; 5SW6; -.
DR PDBsum; 5SX0; -.
DR PDBsum; 5SX1; -.
DR PDBsum; 5SX2; -.
DR PDBsum; 5SX3; -.
DR PDBsum; 5SX6; -.
DR PDBsum; 5SX7; -.
DR PDBsum; 5SXQ; -.
DR PDBsum; 5SXR; -.
DR PDBsum; 5SXS; -.
DR PDBsum; 5SXT; -.
DR PDBsum; 5SXW; -.
DR PDBsum; 5SXX; -.
DR PDBsum; 5SYH; -.
DR PDBsum; 5SYI; -.
DR PDBsum; 5SYJ; -.
DR PDBsum; 5SYK; -.
DR PDBsum; 5SYL; -.
DR PDBsum; 5SYU; -.
DR PDBsum; 5SYV; -.
DR PDBsum; 5SYW; -.
DR PDBsum; 5SYY; -.
DR PDBsum; 5TXQ; -.
DR PDBsum; 5V4O; -.
DR PDBsum; 5V53; -.
DR PDBsum; 6B9B; -.
DR PDBsum; 6CAW; -.
DR PDBsum; 6CC6; -.
DR PDBsum; 6CDQ; -.
DR PDBsum; 6CEK; -.
DR AlphaFoldDB; Q3JNW6; -.
DR SMR; Q3JNW6; -.
DR PeroxiBase; 3313; BpCP01_1710b.
DR EnsemblBacteria; ABA50840; ABA50840; BURPS1710b_3366.
DR KEGG; bpm:BURPS1710b_3366; -.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR BRENDA; 1.11.1.21; 1031.
DR Proteomes; UP000002700; Chromosome I.
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 InterPro; IPR019793; Peroxidases_heam-ligand_BS.
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; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase.
FT CHAIN 1..728
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354748"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 259
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 /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT SITE 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..218
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 244)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 218..244
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5KSK"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5SXW"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:5L02"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5SXQ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5KQK"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5SXW"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5KQ6"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:5SXW"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 376..387
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 389..405
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:5SXQ"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:5SXW"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 498..517
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 527..545
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:5SYH"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 608..621
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 643..648
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:5SXW"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:5SXW"
FT STRAND 675..680
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 690..699
FT /evidence="ECO:0007829|PDB:5SXW"
FT HELIX 705..720
FT /evidence="ECO:0007829|PDB:5SXW"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:5SXW"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:5SXW"
SQ SEQUENCE 728 AA; 79446 MW; FB6EC6E5261F6740 CRC64;
MSNEAKCPFH QAAGNGTSNR DWWPNQLDLS ILHRHSSLSD PMGKDFNYAQ AFEKLDLAAV
KRDLHALMTT SQDWWPADFG HYGGLFIRMA WHSAGTYRTA DGRGGAGEGQ QRFAPLNSWP
DNANLDKARR LLWPIKQKYG RAISWADLLI LTGNVALESM GFKTFGFAGG RADTWEPEDV
YWGSEKIWLE LSGGPNSRYS GDRQLENPLA AVQMGLIYVN PEGPDGNPDP VAAARDIRDT
FARMAMNDEE TVALIAGGHT FGKTHGAGPA SNVGAEPEAA GIEAQGLGWK SAYRTGKGAD
AITSGLEVTW TTTPTQWSHN FFENLFGYEW ELTKSPAGAH QWVAKGADAV IPDAFDPSKK
HRPTMLTTDL SLRFDPAYEK ISRRFHENPE QFADAFARAW FKLTHRDMGP RARYLGPEVP
AEVLLWQDPI PAVDHPLIDA ADAAELKAKV LASGLTVSQL VSTAWAAAST FRGSDKRGGA
NGARIRLAPQ KDWEANQPEQ LAAVLETLEA IRTAFNGAQR GGKQVSLADL IVLAGCAGVE
QAAKNAGHAV TVPFAPGRAD ASQEQTDVES MAVLEPVADG FRNYLKGKYR VPAEVLLVDK
AQLLTLSAPE MTVLLGGLRV LGANVGQSRH GVFTAREQAL TNDFFVNLLD MGTEWKPTAA
DADVFEGRDR ATGELKWTGT RVDLVFGSHS QLRALAEVYG SADAQEKFVR DFVAVWNKVM
NLDRFDLA
