ID A0A4S4LL58_9AGAM Unreviewed; 1724 AA.
AC A0A4S4LL58;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=EW146_g7288 {ECO:0000313|EMBL:THH12864.1};
OS Bondarzewia mesenterica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Bondarzewiaceae; Bondarzewia.
OX NCBI_TaxID=1095465 {ECO:0000313|EMBL:THH12864.1, ECO:0000313|Proteomes:UP000310158};
RN [1] {ECO:0000313|EMBL:THH12864.1, ECO:0000313|Proteomes:UP000310158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108281 {ECO:0000313|EMBL:THH12864.1,
RC ECO:0000313|Proteomes:UP000310158};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Bondarzewia mesenterica.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001270};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2,
CC ECO:0000256|RuleBase:RU363051};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR601621-
CC 2, ECO:0000256|RuleBase:RU363051};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR601621-2};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004374}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000256|ARBA:ARBA00006089, ECO:0000256|RuleBase:RU363051}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THH12864.1}.
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DR EMBL; SGPL01000408; THH12864.1; -; Genomic_DNA.
DR Proteomes; UP000310158; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00692; ligninase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR PANTHER; PTHR10465:SF0; TRANSMEMBRANE GTPASE MARF-RELATED; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR601621-2, ECO:0000256|RuleBase:RU363051};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601621-4};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR601621-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601621-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601621-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000310158}.
FT DOMAIN 202..474
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 917..1205
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 922
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-1"
FT BINDING 923
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 936
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 938
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 940
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 1045
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:0000256|PIRSR:PIRSR601621-2"
FT BINDING 1046
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 1063
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 1065
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 1070
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT SITE 918
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-3"
FT DISULFID 877..890
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 889..1172
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 909..990
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 1136..1201
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ SEQUENCE 1724 AA; 186440 MW; F1C66719FEFA5B15 CRC64;
MSQSYFSQPK HSNSSSSVES STMGEAQLKD VQQAYLEHKD RLVNAIDSTK LVLGDLRVFN
KTSWVVRYPQ LREHAQESAT LKRRQGVRRS LSFADDPLTE TEVVISPSLK RTVTLAPIFD
ASEAEADLTE EPAQEDGERL IPASGASDFH VFRLDLKLGS HGTSTSPAAL VHQLEKSSIA
NLLDERIADS IHHIDKLRVR VEDTSSKVLV TGDLNAGKST FVNALLRREV MPVDQQPCTT
AFCEVHDAAE NEGKEEVHVV KDGVLYNAQD GSTFTRAKVS DLEDIVSENE NSEKILKLYL
NDSRNPTESL LNNGIADISL IDAPGLNRDS VKTTALFARQ EEIDVVVFVV SAENHFTLSA
REFLLNASNE KAYVFIVVNK YEHIRDKAKC RRLVLEQIKQ LSPRTYEDAD DLVHFVDSAS
VPGTSSTSDS FGNLEASLRS FVLVKRSKSK LHPASTYLSH LLSDIDLLVG TNAIVAQAEL
DRAKEDLNRA RPVLEKMQNG REALEDGLEA VEEEGAKKTR AKARQMLTDA LDKVGQGLLG
AEKSMVKMPS FPGLLGIWDY ARDVRKALLA SLDSAVKLAE DEARVMTTDG VNKISKLGDE
HLPEGIERSR RVFMPEAMFS VRNGAGKDGR RKSRRTSHGA IVAGGMHGLG IGLAQRSDLL
EPTFLDLFDV HHQFWVHFGD EKEGNGEEES AVGARGLVEG VLRIADLFGN ESARKWAAPV
VGACVVGLTA YFILELPSTI PRTIGRRIKR SLTKPEEGQE ANEEALFVNA HSTRVSRETR
KVLRLASWDL KERFRAAMEE RGKEVKGAEE MEKKASKAAA WFQEVEKRTS DVREQAGLVS
LVYDTSFKGV QAGMTTLIAL TALVSLANAA VIKSVTCPDG VNKATNAACC VLFPIRDDIQ
KRLFDGGECG EEVHESLRLT FHDAIGYSMS RHMGGGADGS IMVFADAELK YHANGGIDDI
IKAQKPFVAK HNISAGDFIQ FAGAVGVSNC PGAPRLEYLF GRPDPIAPAH DLTVPEPFHS
TDEILARLGD AGFSPDEVVA LLSSHSIAAA DDVDPTVPGT PLDSTPFEFD TQFFVETMLD
GTFWPGTGQN EGEAKAPLHG QMRLQSDAAM ARGQSISLRF LPQLPDKLCK DPRTACTWQS
FANGQMHMAT AFKAAMAKLA IVGHDRDELV DCSEVIPTPR PLTRKAHFPA GFSRADVQQA
CDSAPFPTLP TDPGPATSVA PVMAAFLHSS SSRVITWATL KDLWSRPSSS LFLLDLTNFF
YALDPNRLHI TMGVGPNNLL RAHGYYAPAY DDPGLIDHDV TIIGCDILCM VNSFSPSIRS
TDCVGSPFFL LHAFTTALAP IAALLVVSVT SVPVRRDVDP SLVPDLGFHA GALNANVAVG
HAVNNPPIAV TFPIDNSKAS QSARITASLI TLQNLHGPGV GCPAVSTTLV AQQNAINAAP
AKRATATEIA QLAPDLGFHS GVNPTGTGDC DGAVNGANGQ PIKIPCACPP DRDTFIQHLT
ADVNAGHAVN NPSVPVTFPT DNSKASQSAR ITASLIALQN LNGPGHALDL DMSATNGVPE
DNGDAGRPLF LANVRTQSSF DEIPVIDLHG GKVQDAALRR GVADQIRDAC INIGFFYVRD
HGIPEEIIAG ALGAAKQFFA LPMDTKKELD IHKTANFKGY TALLGENTNP ENRGDLHEGF
DLGWESRTAS GPDVLERVES AMAGGNIWPA EPDAPGFRQA ALNY
//
