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Protein

Leghemoglobin reductase

Gene

FLBR

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reduces ferric leghemoglobin (Lb) to ferrous Lb.1 Publication

Catalytic activityi

NAD(P)H + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei84FADBy similarity1
Binding sitei148FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei237NADBy similarity1
Binding sitei271NAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei306NAD; via amide nitrogenBy similarity1
Binding sitei347FADBy similarity1
Active sitei479Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 75FADBy similarity10
Nucleotide bindingi177 – 179FADBy similarity3
Nucleotide bindingi214 – 221NADBy similarity8
Nucleotide bindingi353 – 356FADBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Leghemoglobin reductase (EC:1.6.2.6)
Alternative name(s):
Ferric leghemoglobin reductase
Short name:
FLbR
Gene namesi
Name:FLBR
OrganismiGlycine max (Soybean) (Glycine hispida)
Taxonomic identifieri3847 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
Proteomesi
  • UP000008827 Componenti: Unplaced

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30Mitochondrion1 PublicationAdd BLAST30
ChainiPRO_000042413731 – 523Leghemoglobin reductaseAdd BLAST493

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi75 ↔ 80Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ41219.
ProMEXiQ41219.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in leaf and nodules.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ41219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

KOiK00382.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q41219-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMANLARRK GYAVVLSSRS SLCLTRWRGF ASGSDENDVV VIGGGPGGYV
60 70 80 90 100
AAIKAAQLGL KTTCIEKRGT LGGTCLNVGC IPSKALLHSS HMYHEAKHAF
110 120 130 140 150
ANHGVKFSSV EVALPAMMGQ KDKAVSNLTQ GIDGLFQKNK VTYVKGYGKL
160 170 180 190 200
VSPSEISVDT TEGENTVVKG KHIIIATGSD VKSLPGVTID EKKIVSSTGA
210 220 230 240 250
LALSEIPKKL VVIGAGYIGL EMGSVWGRIG SEVTVVEFAS EIVPTMDADI
260 270 280 290 300
RKQFQRSLEK QGMKFKLKTK VVGVDTSGDG VKLTVEPSAG GEQTIIEADV
310 320 330 340 350
VLVSAGRTPF TSGLNLDKIG VETDKLGRIL VNERFSTNVS GVYAIGDVIP
360 370 380 390 400
GPMLAHKAEE DGVACVEYLT GKVGHVDYDK VPGVVYTNPE VASVGKTEEQ
410 420 430 440 450
VKETGVEYRV GKFPFLANSR AKAIDNAEGL VKIIAEKETD KILGVHIMAP
460 470 480 490 500
NAGELIHEAA IALQYDASSE DIARVCHAHP TMSEAVKEAA MATYDKPHSH
510 520
LKSWLLLSSL VFIFVQEFTM TWR
Length:523
Mass (Da):55,804
Last modified:November 1, 1996 - v1
Checksum:i4281E1412358673F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S70187 mRNA. Translation: AAB30526.1.
PIRiT08854.
RefSeqiNP_001238628.1. NM_001251699.1.
UniGeneiGma.37081.

Genome annotation databases

GeneIDi547832.
KEGGigmx:547832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S70187 mRNA. Translation: AAB30526.1.
PIRiT08854.
RefSeqiNP_001238628.1. NM_001251699.1.
UniGeneiGma.37081.

3D structure databases

ProteinModelPortaliQ41219.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ41219.
ProMEXiQ41219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi547832.
KEGGigmx:547832.

Phylogenomic databases

KOiK00382.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEGRE_SOYBN
AccessioniPrimary (citable) accession number: Q41219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.