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Protein

FMN-binding protein

Gene

DvMF_2023

Organism
Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a redox protein with a potential of -325 mV.

Cofactori

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciDVUL883:GCJ5-2076-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
FMN-binding protein
Gene namesi
Ordered Locus Names:DvMF_2023
OrganismiDesulfovibrio vulgaris (strain Miyazaki F / DSM 19637)
Taxonomic identifieri883 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000001361 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122FMN-binding proteinPRO_0000087315Add
BLAST

Interactioni

Subunit structurei

Monomer and homodimer.

Protein-protein interaction databases

STRINGi883.DvMF_2023.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Beta strandi15 – 217Combined sources
Beta strandi23 – 3210Combined sources
Helixi33 – 353Combined sources
Beta strandi37 – 393Combined sources
Turni40 – 423Combined sources
Beta strandi43 – 508Combined sources
Helixi52 – 609Combined sources
Beta strandi63 – 7412Combined sources
Beta strandi76 – 9520Combined sources
Helixi96 – 994Combined sources
Turni100 – 1034Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi108 – 12013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXJNMR-A1-122[»]
1FLMX-ray1.30A/B1-122[»]
1WLIX-ray1.60A/B1-122[»]
1WLKX-ray1.90A/B/C/D1-122[»]
2E83X-ray1.52A/B1-122[»]
3A20X-ray1.60A/B1-122[»]
3A6QX-ray1.40A/B1-122[»]
3A6RX-ray1.20A/B/C/D1-122[»]
3AMFX-ray1.60A/B1-122[»]
3AWHX-ray1.60A/B1-122[»]
3VY2X-ray1.60A/B1-122[»]
3VY5X-ray1.40A/B1-122[»]
3VYAX-ray2.40A1-122[»]
ProteinModelPortaliQ46604.
SMRiQ46604. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46604.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG41090Y0. Bacteria.
ENOG4111QUC. LUCA.
HOGENOMiHOG000149904.
OMAiVLKHEGP.
OrthoDBiPOG091H10M0.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR011576. Pyridox_Oxase_FMN-bd.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.

Sequencei

Sequence statusi: Complete.

Q46604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPGTFFEVL KNEGVVAIAT QGEDGPHLVN TWNSYLKVLD GNRIVVPVGG
60 70 80 90 100
MHKTEANVAR DERVLMTLGS RKVAGRNGPG TGFLIRGSAA FRTDGPEFEA
110 120
IARFKWARAA LVITVVSAEQ TL
Length:122
Mass (Da):13,137
Last modified:July 15, 1998 - v2
Checksum:i48F67A37773A3528
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011I → Y AA sequence (PubMed:8119891).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21804 Genomic DNA. Translation: BAA25177.1.
CP001197 Genomic DNA. Translation: ACL08966.1.
PIRiC53203.
RefSeqiWP_012613139.1. NC_011769.1.

Genome annotation databases

EnsemblBacteriaiACL08966; ACL08966; DvMF_2023.
KEGGidvm:DvMF_2023.
PATRICi21774293. VBIDesVul86729_2166.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21804 Genomic DNA. Translation: BAA25177.1.
CP001197 Genomic DNA. Translation: ACL08966.1.
PIRiC53203.
RefSeqiWP_012613139.1. NC_011769.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXJNMR-A1-122[»]
1FLMX-ray1.30A/B1-122[»]
1WLIX-ray1.60A/B1-122[»]
1WLKX-ray1.90A/B/C/D1-122[»]
2E83X-ray1.52A/B1-122[»]
3A20X-ray1.60A/B1-122[»]
3A6QX-ray1.40A/B1-122[»]
3A6RX-ray1.20A/B/C/D1-122[»]
3AMFX-ray1.60A/B1-122[»]
3AWHX-ray1.60A/B1-122[»]
3VY2X-ray1.60A/B1-122[»]
3VY5X-ray1.40A/B1-122[»]
3VYAX-ray2.40A1-122[»]
ProteinModelPortaliQ46604.
SMRiQ46604. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi883.DvMF_2023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL08966; ACL08966; DvMF_2023.
KEGGidvm:DvMF_2023.
PATRICi21774293. VBIDesVul86729_2166.

Phylogenomic databases

eggNOGiENOG41090Y0. Bacteria.
ENOG4111QUC. LUCA.
HOGENOMiHOG000149904.
OMAiVLKHEGP.
OrthoDBiPOG091H10M0.

Enzyme and pathway databases

BioCyciDVUL883:GCJ5-2076-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ46604.
PROiQ46604.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR011576. Pyridox_Oxase_FMN-bd.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFMNB_DESVM
AccessioniPrimary (citable) accession number: Q46604
Secondary accession number(s): B8DML0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: September 7, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.