KATG_NEUCR
ID KATG_NEUCR Reviewed; 753 AA.
AC Q8X182; Q7S4Q3;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_03108};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_03108};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_03108};
DE AltName: Full=Catalase-2;
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_03108};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_03108}; Synonyms=cat-2;
GN ORFNames=NCU05770;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 654-670, HEME-BINDING,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=12033445; DOI=10.1515/bc.2002.058;
RA Peraza L., Hansberg W.;
RT "Neurospora crassa catalases, singlet oxygen and cell differentiation.";
RL Biol. Chem. 383:569-575(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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_03108};
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_03108};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
CC {ECO:0000255|HAMAP-Rule:MF_03108};
CC -!- ACTIVITY REGULATION: Inhibited by KCN. {ECO:0000269|PubMed:12033445}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.2 mM for H(2)O(2) for the catalase reaction
CC {ECO:0000269|PubMed:12033445};
CC pH dependence:
CC Optimum pH is 4.75 for the peroxidase reaction and 6.25 for the
CC catalase reaction. {ECO:0000269|PubMed:12033445};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
CC -!- INDUCTION: Induced in late stationary growth phase.
CC {ECO:0000269|PubMed:12033445}.
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_03108}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03108}.
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DR EMBL; AF459787; AAL66352.2; -; mRNA.
DR EMBL; CM002242; EAA30509.1; -; Genomic_DNA.
DR RefSeq; XP_959745.1; XM_954652.3.
DR PDB; 5WHQ; X-ray; 2.90 A; A/B=2-753.
DR PDB; 5WHS; X-ray; 2.60 A; A/B=7-741.
DR PDBsum; 5WHQ; -.
DR PDBsum; 5WHS; -.
DR AlphaFoldDB; Q8X182; -.
DR SMR; Q8X182; -.
DR STRING; 5141.EFNCRP00000005777; -.
DR PeroxiBase; 2181; NcCP01.
DR EnsemblFungi; EAA30509; EAA30509; NCU05770.
DR GeneID; 3875883; -.
DR KEGG; ncr:NCU05770; -.
DR VEuPathDB; FungiDB:NCU05770; -.
DR HOGENOM; CLU_025424_2_0_1; -.
DR InParanoid; Q8X182; -.
DR OMA; MILAGNC; -.
DR BRENDA; 1.11.1.6; 3627.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0005829; C:cytosol; 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:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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; Cytoplasm; Direct protein sequencing; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..753
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055582"
FT REGION 196..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT BINDING 279
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_03108"
FT SITE 87
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 90..238
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 264)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT CROSSLNK 238..264
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 90)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03108"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5WHQ"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5WHS"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5WHS"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:5WHS"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 396..407
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 409..425
FT /evidence="ECO:0007829|PDB:5WHS"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:5WHQ"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 477..488
FT /evidence="ECO:0007829|PDB:5WHS"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 518..536
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 546..560
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 584..588
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 607..617
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 622..634
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:5WHQ"
FT HELIX 657..662
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 667..683
FT /evidence="ECO:0007829|PDB:5WHS"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 689..694
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 695..702
FT /evidence="ECO:0007829|PDB:5WHS"
FT HELIX 704..713
FT /evidence="ECO:0007829|PDB:5WHS"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:5WHQ"
FT HELIX 719..734
FT /evidence="ECO:0007829|PDB:5WHS"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:5WHS"
SQ 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
