ID A0A1E3Q1I8_LIPST Unreviewed; 747 AA.
AC A0A1E3Q1I8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN ORFNames=LIPSTDRAFT_154486 {ECO:0000313|EMBL:ODQ71374.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ71374.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ71374.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ71374.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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:0000256|PIRNR:PIRNR038927};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927}.
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DR EMBL; KV454298; ODQ71374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3Q1I8; -.
DR STRING; 675824.A0A1E3Q1I8; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000094385; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF3; CATALASE B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000094385};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..747
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009134035"
FT DOMAIN 70..457
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 189
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 403
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:0000256|PIRSR:PIRSR038927-2"
SQ SEQUENCE 747 AA; 81641 MW; 799EAF354B65D089 CRC64;
MRGLLLLPSI VGLAAAVGCP YSAAALSGRA VNDNDEISSS QPGQNANTVG ETDPEFLSQY
YLNDTGSYMT TDFGTPIQDQ STLKVGARGP TLLEDFMFRQ KLQRFDHERV PERVVHARGT
GAHGVFTSYG DWSNITAASF LSAEGKQTPV FTRFSTVQGF RGSPDTVRDM HGFATKFYTD
EGNFDLVGNT VPVFFITDAI QFPDIIHAVK PEPRNEIPQG GTAHDNAWDF FSQQPSAMHT
LLWFMAGHGI PHNFRHVNGY GVHTFRLVTA DGASKLVKFH WKSLQGVAAK VWEEAQAAAG
KNIDYMRQDL FNNIAAGRYP EWELGVQIMD ESQMLAFGFD LLDPTKIVPE EYVPITWLGK
MQLNANPMNY FAETEQIAMH PGHIVRGIDF SDDPLLQGRL YSYHDTQINR HGGPNFEQIP
INRPRVPIHN NNRDGFSQQY IPLNNAPYTP NTLDNDSPKQ ANQTVGNGFF TAPGRHASGH
LVRQPAFSDF YSQARLFWNS LVPAEKQFVV NAIVFENSKV TNTVVRQNVI TAINLVDNNL
AVKVAEGLGL PHPKPNPTFY HNNKTCCVGT FGQPVLSVAG MQVGFLASNA YPASITQGMS
MSASFAAAGV DLVVVAETWA EGVNATYSIS DAINFDAVVV AGGVEGLFSV ESFTNQPAKG
KAPPTQVSAT SPLFPAGRPS QILVDAFKYG KPVGALDSGS AALTAFDISL TRPGVYVANS
TTITAFVNEV IRGLYTFKFL DRFELEP
//
