LEGRE_SOYBN
ID LEGRE_SOYBN Reviewed; 523 AA.
AC Q41219;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-80, FUNCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=8159785; DOI=10.1104/pp.104.2.453;
RA Ji L., Becana M., Sarath G., Klucas R.V.;
RT "Cloning and sequence analysis of a cDNA encoding ferric leghemoglobin
RT reductase from soybean nodules.";
RL Plant Physiol. 104:453-459(1994).
CC -!- FUNCTION: Reduces ferric leghemoglobin (Lb) to ferrous Lb.
CC {ECO:0000269|PubMed:8159785}.
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 -!- 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:8159785}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in leaf
CC and nodules. {ECO:0000269|PubMed:8159785}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; S70187; AAB30526.1; -; mRNA.
DR PIR; T08854; T08854.
DR RefSeq; NP_001238628.1; NM_001251699.1.
DR AlphaFoldDB; Q41219; -.
DR SMR; Q41219; -.
DR STRING; 3847.GLYMA07G36040.1; -.
DR PRIDE; Q41219; -.
DR ProMEX; Q41219; -.
DR GeneID; 547832; -.
DR eggNOG; KOG1335; Eukaryota.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0015043; F:leghemoglobin reductase activity; IEA:UniProtKB-EC.
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;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8159785"
FT CHAIN 31..523
FT /note="Leghemoglobin reductase"
FT /id="PRO_0000424137"
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; 55804 MW; 4281E1412358673F CRC64;
MAMANLARRK GYAVVLSSRS SLCLTRWRGF ASGSDENDVV VIGGGPGGYV AAIKAAQLGL
KTTCIEKRGT LGGTCLNVGC IPSKALLHSS HMYHEAKHAF ANHGVKFSSV EVALPAMMGQ
KDKAVSNLTQ GIDGLFQKNK VTYVKGYGKL VSPSEISVDT TEGENTVVKG KHIIIATGSD
VKSLPGVTID EKKIVSSTGA LALSEIPKKL VVIGAGYIGL EMGSVWGRIG SEVTVVEFAS
EIVPTMDADI RKQFQRSLEK QGMKFKLKTK VVGVDTSGDG VKLTVEPSAG GEQTIIEADV
VLVSAGRTPF TSGLNLDKIG VETDKLGRIL VNERFSTNVS GVYAIGDVIP GPMLAHKAEE
DGVACVEYLT GKVGHVDYDK VPGVVYTNPE VASVGKTEEQ VKETGVEYRV GKFPFLANSR
AKAIDNAEGL VKIIAEKETD KILGVHIMAP NAGELIHEAA IALQYDASSE DIARVCHAHP
TMSEAVKEAA MATYDKPHSH LKSWLLLSSL VFIFVQEFTM TWR
