位置:首页 > 蛋白库 > LEGRE_VIGUN
LEGRE_VIGUN
ID   LEGRE_VIGUN             Reviewed;         523 AA.
AC   Q9SPB1;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Leghemoglobin reductase;
DE            EC=1.6.2.6;
DE   AltName: Full=Ferric leghemoglobin reductase;
DE            Short=FLbR;
DE   Flags: Precursor;
GN   Name=FLBR;
OS   Vigna unguiculata (Cowpea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-50, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Root nodule;
RX   PubMed=10729615; DOI=10.1016/s0168-9452(99)00272-1;
RA   Luan P., Arechaga-Ocampo E., Sarath G., Arredondo-Peter R., Klucas R.V.;
RT   "Analysis of a ferric leghemoglobin reductase from cowpea (Vigna
RT   unguiculata) root nodules.";
RL   Plant Sci. 154:161-170(2000).
CC   -!- FUNCTION: Reduces ferric leghemoglobin (Lb) to ferrous Lb.
CC       {ECO:0000269|PubMed:10729615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[leghemoglobin] + NADH = 2 Fe(II)-[leghemoglobin] +
CC         H(+) + NAD(+); Xref=Rhea:RHEA:16161, Rhea:RHEA-COMP:13792, Rhea:RHEA-
CC         COMP:13793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.6;
CC         Evidence={ECO:0000269|PubMed:10729615};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[leghemoglobin] + NADPH = 2 Fe(II)-[leghemoglobin] +
CC         H(+) + NADP(+); Xref=Rhea:RHEA:16157, Rhea:RHEA-COMP:13792,
CC         Rhea:RHEA-COMP:13793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.2.6;
CC         Evidence={ECO:0000269|PubMed:10729615};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.4 uM for ferrileghemoglobin {ECO:0000269|PubMed:10729615};
CC         Vmax=221 nmol/min/mg enzyme {ECO:0000269|PubMed:10729615};
CC         Note=kcat is 3.1 sec(-1).;
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:10729615};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10729615}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:10729615}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF181096; AAD53185.1; -; mRNA.
DR   AlphaFoldDB; Q9SPB1; -.
DR   SMR; Q9SPB1; -.
DR   SABIO-RK; Q9SPB1; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0015043; F:leghemoglobin reductase activity; IDA:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   Mitochondrion; NAD; Oxidoreductase; Redox-active center; Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:10729615"
FT   CHAIN           31..523
FT                   /note="Leghemoglobin reductase"
FT                   /id="PRO_0000424138"
FT   ACT_SITE        479
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..75
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..179
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..221
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         353..356
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..80
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   523 AA;  55780 MW;  87CC889A297E02F8 CRC64;
     MAMASLARRK AYAVVSSSRS SVFLTSLRGF ASGSDENDVV VIGGGPGGYV AAIKASQLGL
     KTTCIEKRGT LGGTCLNVGC IPSKALLHSS HMYHEAKHSF ANHGIKLSSV EVDLAGMMAQ
     KDKAVSNLTK GIEGLFKKNK VNYVKGYGKF VSPSEVSVDT IDGGNTVVKG KHIIIATGSD
     VKSLPGVTID EKKIVSSTGA LALTEIPKKL VVIGAGYIGL EMGSVWGRLG SEVTVVEFAS
     DIVPTMDAEV RKQFQRSLEK QGMKFQLKTK VVGVDTSGDG VKLTLEPAAG GDQTILETDV
     VLVSAGRTPF TAGLGLDKIG VETDKIRRIL VNERFTTNVS GVYAIGDVIP GPMLAHKAEE
     DGVACVEFIA GKVGHVDYDK VPGVVYTTPE VAYVGKTEEQ VKALGVEYRV GKFPFMANSR
     AKAIDNAEGL VKILAEKETD KILGVHIMAP NAGELIHEAA IALQYDASSE DIARVCHAHP
     TMSEAVKEAA MATYDKPHSH MKSWLLLHSL LFIFVQQFTM TWR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024