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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.
OrthoDBiEOG686NQ5.

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.
OrthoDBiEOG686NQ5.

Enzyme and pathway databases

BioCyciDVUL883:GCJ5-2076-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ46604.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Novel FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F). Cloning and expression of its gene in Escherichia coli."
    Kitamura M., Kojima S., Ogasawara K., Nakaya T., Sagara T., Niki K., Miura K., Akutsu H., Kumagai I.
    J. Biol. Chem. 269:5566-5573(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C., Richardson P.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Miyazaki F / DSM 19637.
  3. "Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)."
    Liepinsh E., Kitamura M., Murakami T., Nakaya T., Otting G.
    Nat. Struct. Biol. 4:975-979(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SEQUENCE REVISION TO 101.
  4. "How do the X-ray structure and the NMR structure of FMN-binding protein differ?"
    Suto K., Kawagoe K., Shibata N., Morimoto Y., Higuchi Y., Kitamura M., Nakaya T., Yasuoka N.
    Acta Crystallogr. D 56:368-371(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).

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: December 9, 2015
This is version 106 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.