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F6H12_IPOBA
ID   F6H12_IPOBA             Reviewed;         358 AA.
AC   G9M9M1;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Feruloyl CoA ortho-hydroxylase F6H1-2 {ECO:0000303|PubMed:22169019};
DE            Short=IbF6H1-2 {ECO:0000303|PubMed:22169019};
DE            EC=1.14.11.61 {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:22169019};
DE   AltName: Full=2-oxoglutarate-dependent dioxygenase F6H1-2 {ECO:0000303|PubMed:22169019};
DE            Short=2OGD F6H1-2 {ECO:0000303|PubMed:22169019};
GN   Name=F6H1-2 {ECO:0000303|PubMed:22169019};
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Root tuber;
RX   PubMed=22169019; DOI=10.1016/j.phytochem.2011.11.009;
RA   Matsumoto S., Mizutani M., Sakata K., Shimizu B.;
RT   "Molecular cloning and functional analysis of the ortho-hydroxylases of p-
RT   coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of
RT   umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam.";
RL   Phytochemistry 74:49-57(2012).
CC   -!- FUNCTION: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD)
CC       involved in scopoletin biosynthesis (PubMed:22169019). Converts
CC       feruloyl CoA into 6'-hydroxyferuloyl CoA, and, at low efficiency,
CC       caffeoyl-CoA into 6'-hydroxycaffeate, but has no activity with p-
CC       coumaroyl-CoA (PubMed:22169019). {ECO:0000269|PubMed:22169019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-feruloyl-CoA + 2-oxoglutarate + O2 = (E)-6-
CC         hydroxyferuloyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:57856,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:87305, ChEBI:CHEBI:142390;
CC         EC=1.14.11.61; Evidence={ECO:0000269|PubMed:22169019};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000250|UniProtKB:Q9C899};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.15 uM for feruloyl-CoA {ECO:0000269|PubMed:22169019};
CC         Note=kcat is 2.68 sec(-1) with feruloyl-CoA as substrate.
CC         {ECO:0000269|PubMed:22169019};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:22169019};
CC   -!- PATHWAY: Phenylpropanoid metabolism. {ECO:0000269|PubMed:22169019}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in tubers, underground
CC       stems, leaves and petioles. {ECO:0000269|PubMed:22169019}.
CC   -!- INDUCTION: Transiently induced by fungal (F.oxysporum f.sp. batatas O-
CC       17) and chitosan treatments, in association with the accumulation of
CC       umbelliferone and its glucoside (skimmin) in the tubers.
CC       {ECO:0000269|PubMed:22169019}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB636150; BAL22344.1; -; mRNA.
DR   AlphaFoldDB; G9M9M1; -.
DR   SMR; G9M9M1; -.
DR   BRENDA; 1.14.11.61; 2773.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009805; P:coumarin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..358
FT                   /note="Feruloyl CoA ortho-hydroxylase F6H1-2"
FT                   /id="PRO_0000447354"
FT   DOMAIN          200..308
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         216
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:D4N500"
FT   BINDING         231
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         233
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         289
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         299
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         301
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:D4N500"
SQ   SEQUENCE   358 AA;  39934 MW;  20E38C691B87A0FE CRC64;
     MPAVLSSVLS NITDFVVHEG NGVKGLADMG LEALPKQYVQ PEEERITTST VIVDDTIPVI
     DLSEWGSDPK VGDMICEAAE KWGFFQIVNH GVPLEVLEEV KAATYRFFRL PAEEKNKHCK
     DNSPSNNVRY GTSFTPHAEK ALEWKDFLSL FYVSDEEAAA LWPSACRDEA LTFMRNCDAV
     IKRLLKSLMK GLNVTEIDGT KESLLMGSKR INMNYYPKCP NPELTVGVGR HSDVSTLTIL
     LQDQIGGLYV RKLDSDTWVH VPPINGAIVI NVGDALQILS NGRYKSIEHR VIANGSNNRI
     SVPIFVNPRP NDIIGPLPEL LESGEKAVYK NVLYSDYVKH FFRKAHDGKE TVDFAKIN
 
 
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