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 13-SEP-2023, entry version 114.
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}.
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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 Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF221; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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
//
