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Catalase-peroxidase (CP) (EC 1.11.1.21) (Catalase-2) (Peroxidase/catalase)

 KATG_NEUCR              Reviewed;         753 AA.
Q8X182; Q7S4Q3;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
28-MAR-2018, entry version 115.
RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_03108};
Short=CP {ECO:0000255|HAMAP-Rule:MF_03108};
EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
AltName: Full=Catalase-2;
AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_03108};
Name=katG {ECO:0000255|HAMAP-Rule:MF_03108}; Synonyms=cat-2;
ORFNames=NCU05770;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 654-670, HEME-BINDING,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND INDUCTION.
PubMed=12033445; DOI=10.1515/BC.2002.058;
Peraza L., Hansberg W.;
"Neurospora crassa catalases, singlet oxygen and cell
differentiation.";
Biol. Chem. 383:569-575(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
-!- FUNCTION: Bifunctional enzyme with both catalase and broad-
spectrum peroxidase activity.
-!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_03108}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_03108}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
monomer. {ECO:0000255|HAMAP-Rule:MF_03108};
-!- ENZYME REGULATION: Inhibited by KCN.
{ECO:0000269|PubMed:12033445}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13.2 mM for H(2)O(2) for the catalase reaction
{ECO:0000269|PubMed:12033445};
pH dependence:
Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the
catalase reaction. {ECO:0000269|PubMed:12033445};
-!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-
Rule:MF_03108}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
-!- INDUCTION: Induced in late stationary growth phase.
{ECO:0000269|PubMed:12033445}.
-!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is
important for the catalase, but not the peroxidase activity of the
enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}.
-!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
subfamily. {ECO:0000255|HAMAP-Rule:MF_03108}.
-----------------------------------------------------------------------
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EMBL; AF459787; AAL66352.2; -; mRNA.
EMBL; CM002242; EAA30509.1; -; Genomic_DNA.
RefSeq; XP_959745.1; XM_954652.3.
PDB; 5WHQ; X-ray; 2.90 A; A/B=2-753.
PDB; 5WHS; X-ray; 2.60 A; A/B=7-741.
PDBsum; 5WHQ; -.
PDBsum; 5WHS; -.
ProteinModelPortal; Q8X182; -.
SMR; Q8X182; -.
PeroxiBase; 2181; NcCP01.
PRIDE; Q8X182; -.
EnsemblFungi; EAA30509; EAA30509; NCU05770.
GeneID; 3875883; -.
KEGG; ncr:NCU05770; -.
EuPathDB; FungiDB:NCU05770; -.
HOGENOM; HOG000218110; -.
InParanoid; Q8X182; -.
KO; K03782; -.
OMA; PEEDIYW; -.
OrthoDB; EOG092C0YTX; -.
BRENDA; 1.11.1.6; 3627.
Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IBA:GO_Central.
GO; GO:0004096; F:catalase activity; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
HAMAP; MF_01961; Catal_peroxid; 1.
InterPro; IPR000763; Catalase_peroxidase.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
PANTHER; PTHR30555; PTHR30555; 1.
Pfam; PF00141; peroxidase; 2.
PRINTS; PR00460; BPEROXIDASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 2.
TIGRFAMs; TIGR00198; cat_per_HPI; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
Peroxidase; Reference proteome.
CHAIN 1 753 Catalase-peroxidase.
/FTId=PRO_0000055582.
ACT_SITE 91 91 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03108}.
METAL 279 279 Iron (heme axial ligand).
{ECO:0000255|HAMAP-Rule:MF_03108}.
SITE 87 87 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_03108}.
CROSSLNK 90 238 Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
(with M-264). {ECO:0000255|HAMAP-
Rule:MF_03108}.
CROSSLNK 238 264 Tryptophyl-tyrosyl-methioninium (Tyr-Met)
(with W-90). {ECO:0000255|HAMAP-
Rule:MF_03108}.
HELIX 18 21 {ECO:0000244|PDB:5WHS}.
HELIX 29 31 {ECO:0000244|PDB:5WHS}.
HELIX 36 38 {ECO:0000244|PDB:5WHS}.
HELIX 47 52 {ECO:0000244|PDB:5WHS}.
HELIX 56 66 {ECO:0000244|PDB:5WHS}.
STRAND 72 74 {ECO:0000244|PDB:5WHQ}.
HELIX 77 79 {ECO:0000244|PDB:5WHS}.
HELIX 82 89 {ECO:0000244|PDB:5WHS}.
HELIX 93 95 {ECO:0000244|PDB:5WHS}.
TURN 98 100 {ECO:0000244|PDB:5WHS}.
HELIX 109 111 {ECO:0000244|PDB:5WHS}.
HELIX 115 117 {ECO:0000244|PDB:5WHS}.
HELIX 124 130 {ECO:0000244|PDB:5WHS}.
HELIX 132 138 {ECO:0000244|PDB:5WHS}.
HELIX 139 141 {ECO:0000244|PDB:5WHS}.
HELIX 144 158 {ECO:0000244|PDB:5WHS}.
STRAND 166 168 {ECO:0000244|PDB:5WHS}.
TURN 192 194 {ECO:0000244|PDB:5WHS}.
STRAND 237 239 {ECO:0000244|PDB:5WHS}.
HELIX 244 246 {ECO:0000244|PDB:5WHS}.
HELIX 250 262 {ECO:0000244|PDB:5WHS}.
TURN 263 265 {ECO:0000244|PDB:5WHS}.
HELIX 268 278 {ECO:0000244|PDB:5WHS}.
HELIX 290 292 {ECO:0000244|PDB:5WHS}.
HELIX 297 299 {ECO:0000244|PDB:5WHS}.
HELIX 302 304 {ECO:0000244|PDB:5WHS}.
HELIX 318 320 {ECO:0000244|PDB:5WHS}.
STRAND 322 325 {ECO:0000244|PDB:5WHS}.
HELIX 340 347 {ECO:0000244|PDB:5WHS}.
STRAND 348 354 {ECO:0000244|PDB:5WHS}.
STRAND 360 366 {ECO:0000244|PDB:5WHS}.
HELIX 387 394 {ECO:0000244|PDB:5WHS}.
HELIX 396 407 {ECO:0000244|PDB:5WHS}.
HELIX 409 425 {ECO:0000244|PDB:5WHS}.
TURN 426 428 {ECO:0000244|PDB:5WHQ}.
HELIX 431 433 {ECO:0000244|PDB:5WHS}.
STRAND 435 438 {ECO:0000244|PDB:5WHS}.
HELIX 460 472 {ECO:0000244|PDB:5WHS}.
HELIX 477 488 {ECO:0000244|PDB:5WHS}.
TURN 493 496 {ECO:0000244|PDB:5WHS}.
HELIX 504 506 {ECO:0000244|PDB:5WHS}.
HELIX 510 512 {ECO:0000244|PDB:5WHS}.
HELIX 514 516 {ECO:0000244|PDB:5WHS}.
HELIX 518 536 {ECO:0000244|PDB:5WHS}.
STRAND 537 539 {ECO:0000244|PDB:5WHS}.
HELIX 546 560 {ECO:0000244|PDB:5WHS}.
HELIX 577 579 {ECO:0000244|PDB:5WHS}.
HELIX 584 588 {ECO:0000244|PDB:5WHS}.
HELIX 594 596 {ECO:0000244|PDB:5WHS}.
STRAND 603 605 {ECO:0000244|PDB:5WHS}.
HELIX 607 617 {ECO:0000244|PDB:5WHS}.
HELIX 622 634 {ECO:0000244|PDB:5WHS}.
HELIX 639 641 {ECO:0000244|PDB:5WHQ}.
HELIX 657 662 {ECO:0000244|PDB:5WHS}.
STRAND 667 683 {ECO:0000244|PDB:5WHS}.
TURN 684 686 {ECO:0000244|PDB:5WHS}.
STRAND 689 694 {ECO:0000244|PDB:5WHS}.
HELIX 695 702 {ECO:0000244|PDB:5WHS}.
HELIX 704 713 {ECO:0000244|PDB:5WHS}.
STRAND 715 717 {ECO:0000244|PDB:5WHQ}.
HELIX 719 734 {ECO:0000244|PDB:5WHS}.
TURN 735 737 {ECO:0000244|PDB:5WHS}.
SEQUENCE 753 AA; 83380 MW; DED01DC6D10BA582 CRC64;
MSECPVRKSN VGGGGTRNHD WWPAQLRLNI LRQHTPVSNP LDKDFDYAAA FKSLDYEGLK
KDLTKLMTDS QDWWPADFGH YGGLFIRMAW HSAGTYRVTD GRGGGGEGQQ RFAPLNSWPD
NVSLDKARRL LWPIKQKYGN KISWSDLLLL TGNVALESMG FKTFGFAGGR PDTWEADESV
YWGAETTWLG NEDRYSEGQE GHEGHGVVQG DESKKQHTDI HNRDLQSPLA SSHMGLIYVN
PEGPDGIPDP VASAKDIRVT FGRMAMNDEE TVALIAGGHS FGKTHGAGPT HHVGKEPEAA
PIEHQGLGWA NSFGQGKGPD TITSGLEVTW TPTPTKWGMG YLEYLYKFDW EPTKSPAGAN
QWVAKNAEPT IPDAYDPNKK KLPTMLTTDI ALRMDPAYDK ICRDYLANPD KFADAFARAW
FKLLHRDMGP RTRWIGPEVP SEILPWEDYI PPVDYQIIDD NDIAALKKEI LATGVAPKKL
IFVAWSSASS FRGSDKRGGA NGARIRLAPQ NEWKVNDPST LREVLAALES VQQKFNDSSS
GKKVSLADLI VLGGVAALEQ ASGLVVPFTP GRNDATQEHT DVHSFTHLEP HADGFRSYGK
GTKRVRTEQF LIDRASLLTL SAPELTALIG GLRVLEANYD GSSYGVLTKT PGKLTNDYFV
NLLDTNTAWK AADNEGEVFI GYDRKTHDKK WTATRADLIF GAHAELRALA EVYAAVDGEE
KFKRDFVAAW HKVMNLDRFD LKQEGRGQNA PKL


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