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PPOA_EMEND
ID   PPOA_EMEND              Reviewed;        1081 AA.
AC   Q6RET3; Q5BBW3;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Psi-producing oxygenase A;
DE   AltName: Full=Fatty acid oxygenase ppoA;
DE   Includes:
DE     RecName: Full=Linoleate 8R-lipoxygenase;
DE              EC=1.13.11.60;
DE   Includes:
DE     RecName: Full=9,12-octadecadienoate 8-hydroperoxide 8R-isomerase;
DE              EC=5.4.4.5;
GN   Name=ppoA;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=14699095; DOI=10.1074/jbc.m310840200;
RA   Tsitsigiannis D.I., Zarnowski R., Keller N.P.;
RT   "The lipid body protein, PpoA, coordinates sexual and asexual sporulation
RT   in Aspergillus nidulans.";
RL   J. Biol. Chem. 279:11344-11353(2004).
RN   [2]
RP   SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-374 AND HIS-1004.
RX   PubMed=19286665; DOI=10.1074/jbc.m809152200;
RA   Brodhun F., Gobel C., Hornung E., Feussner I.;
RT   "Identification of PpoA from Aspergillus nidulans as a fusion protein of a
RT   fatty acid heme dioxygenase/peroxidase and a cytochrome P450.";
RL   J. Biol. Chem. 284:11792-11805(2009).
CC   -!- FUNCTION: Bifunctional heme-containing enzyme that oxidizes linoleic
CC       acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-
CC       terminal heme peroxidase domain), which is subsequently isomerized to
CC       (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-
CC       terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids,
CC       so-called oxylipins, derived from endogenous fatty acids, influence the
CC       development of the asexual conidiophores and sexual cleistothecia and
CC       regulate the secondary metabolism. These substances were collectively
CC       named psi factors and are primarily a mixture of hydroxylated oleic,
CC       linoleic and alpha-linolenic acids. They are termed psi-beta, psi-
CC       alpha, and psi-gamma, respectively. {ECO:0000269|PubMed:14699095}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-
CC         hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659;
CC         EC=1.13.11.60; Evidence={ECO:0000269|PubMed:19286665};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate =
CC         (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate;
CC         Xref=Rhea:RHEA:31579, ChEBI:CHEBI:58659, ChEBI:CHEBI:63217;
CC         EC=5.4.4.5; Evidence={ECO:0000269|PubMed:19286665};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:19286665};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 uM for palmitoleic acid {ECO:0000269|PubMed:19286665};
CC         KM=6.71 uM for oleic acid {ECO:0000269|PubMed:19286665};
CC         KM=18.3 uM for linoleic acid {ECO:0000269|PubMed:19286665};
CC         KM=22.6 uM for alpha-linolenic acid {ECO:0000269|PubMed:19286665};
CC         Vmax=1.76 umol/min/mg enzyme toward palmitoleic acid
CC         {ECO:0000269|PubMed:19286665};
CC         Vmax=2.48 umol/min/mg enzyme toward oleic acid
CC         {ECO:0000269|PubMed:19286665};
CC         Vmax=3.16 umol/min/mg enzyme toward linoleic acid
CC         {ECO:0000269|PubMed:19286665};
CC         Vmax=2.97 umol/min/mg enzyme toward alpha-linolenic acid
CC         {ECO:0000269|PubMed:19286665};
CC       pH dependence:
CC         Optimum pH is 7-7.5. {ECO:0000269|PubMed:19286665};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19286665}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00298}.
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DR   EMBL; AY502073; AAR88626.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6RET3; -.
DR   SASBDB; Q6RET3; -.
DR   SMR; Q6RET3; -.
DR   PeroxiBase; 5297; AniLDS01.
DR   OMA; NEFRKYF; -.
DR   BRENDA; 1.13.11.60; 517.
DR   BRENDA; 5.4.4.5; 517.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0052878; F:linoleate 8R-lipoxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; -; 1.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR034812; Ppo_N.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF00067; p450; 1.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Heme; Iron; Isomerase; Metal-binding; Multifunctional enzyme;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN           1..1081
FT                   /note="Psi-producing oxygenase A"
FT                   /id="PRO_0000416225"
FT   REGION          105..446
FT                   /note="Linoleate 8R-lipoxygenase"
FT   REGION          654..1081
FT                   /note="9,12-octadecadienoate 8-hydroperoxide 8R-isomerase"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000255"
FT   BINDING         202
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|PROSITE-ProRule:PRU00298"
FT   BINDING         377
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|PROSITE-ProRule:PRU00298"
FT   MUTAGEN         374
FT                   /note="Y->F: Impairs the linoleate 8R-lipoxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:19286665"
FT   MUTAGEN         1004
FT                   /note="H->A: Impairs the isomerase activity."
FT                   /evidence="ECO:0000269|PubMed:19286665"
SQ   SEQUENCE   1081 AA;  120784 MW;  4F967A2E368C12B6 CRC64;
     MGEDKETNIL AGLGNTISQV ENVVAASLRP LPTATGDGTY VAESTQTGLA KDLSHVDLKD
     VRTLAEVVKS AATGEPVDDK QYIMERVIQL AAGLPSTSRN AAELTKSFLN MLWNDLEHPP
     VSYLGADSMH RKADGSGNNR FWPQLGAAGS AYARSVRPKT MQSPSLPDPE TIFDCLLRRK
     EYREHPNKIS SVLFYLASII IHDLFQTDPK DNSVSKTSSY LDLSPLYGNN QDEQNLVRTF
     KDGKLKPDCF ATKRVLGFPP GVGVLLIMFN RFHNYVVDQL AAINECGRFT KPDESNVDEY
     AKYDNNLFQT GRLVTCGLYA NIILKDYVRT ILNINRTDST WSLDPRMEMK DGLLGEAAAM
     ATGNQVSAEF NVVYRWHACI SKRDEKWTED FHREIMPGVD PSTLSMQDFV AGLGRWQAGL
     PQEPLERPFS GLQRKPDGAF NDDDLVNLFE KSVEDCAGAF GASHVPAIFK SVEALGIMQA
     RRWNLGTLNE FRQYFNLAPH KTFEDINSDP YIADQLKRLY DHPDLVEIYP GVVVEEAKDS
     MVPGSGLCTN FTISRAILSD AVALVRGDRF YTVDYTPKHL TNWAYNEIQP NNAVDQGQVF
     YKLVLRAFPN HFDGNSIYAH FPLVVPSENE KILKSLGVAE KYSWEKPSRI SHPIFISSHA
     ACMSILENQE TFKVTWGRKI EFLMQRDKHQ YGKDFMLSGD RPPNAASRKM MGSALYRDEW
     EAEVKNFYEQ TTLKLLHKNS YKLAGVNQVD IVRDVANLAQ VHFCSSVFSL PLKTDSNPRG
     IFAESELYKI MAAVFTAIFY DADIGKSFEL NQAARTVTQQ LGQLTMANVE IIAKTGLIAN
     LVNRLHRRDV LSEYGIHMIQ RLLDSGLPAT EIVWTHILPT AGGMVANQAQ LFSQCLDYYL
     SEEGSGHLPE INRLAKENTP EADELLTRYF MEGARLRSSV ALPRVAAQPT VVEDNGEKLT
     IKAGQVVMCN LVSACMDPTA FPDPEKVKLD RDMNLYAHFG FGPHKCLGLD LCKTGLSTML
     KVLGRLDNLR RAPGAQGQLK KLSGPGGIAK YMNEDQSGFT PFPSTMKIQW DGELPQLKED
     F
 
 
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