Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Riboflavin biosynthesis protein

Gene

TM_0857

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + FMN = diphosphate + FAD.UniRule annotation
ATP + riboflavin = ADP + FMN.UniRule annotation

Pathwayi: FAD biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Riboflavin biosynthesis protein (TM_0857)
This subpathway is part of the pathway FAD biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes FAD from FMN, the pathway FAD biosynthesis and in Cofactor biosynthesis.

Pathwayi: FMN biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FMN from riboflavin (ATP route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Riboflavin biosynthesis protein (TM_0857)
This subpathway is part of the pathway FMN biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes FMN from riboflavin (ATP route), the pathway FMN biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351AMP; via carbonyl oxygenCombined sources
Binding sitei215 – 2151FMNCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 82AMPCombined sources
Nucleotide bindingi12 – 154AMPCombined sources
Nucleotide bindingi99 – 1013AMPCombined sources
Nucleotide bindingi127 – 1282AMPCombined sources
Nucleotide bindingi179 – 1824ADPCombined sources
Nucleotide bindingi231 – 24212ADPCombined sourcesAdd
BLAST
Nucleotide bindingi255 – 2584FMNCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationImported, NucleotidyltransferaseUniRule annotationImported, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotation, FADUniRule annotation, Flavoprotein, FMNUniRule annotationCombined sources, Nucleotide-binding

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-887-MONOMER.
UniPathwayiUPA00276; UER00406.
UPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin biosynthesis proteinUniRule annotation (EC:2.7.1.26UniRule annotation, EC:2.7.7.2UniRule annotation)
Gene namesi
Ordered Locus Names:TM_0857Imported
ORF Names:Tmari_0859Imported
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)Imported
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000013901 Componenti: Chromosome
  • UP000008183 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi243274.TM0857.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRZX-ray1.90A/B1-293[»]
1S4MX-ray2.10A/B1-293[»]
1T6XX-ray2.29A/B1-293[»]
1T6YX-ray2.80A/B1-293[»]
1T6ZX-ray2.40A/B1-293[»]
2I1LX-ray2.50A/B1-293[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini155 – 282128FlavokinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribF family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DTN. Bacteria.
COG0196. LUCA.
KOiK11753.
OMAiFPTANMR.
OrthoDBiEOG6QP0ZV.

Family and domain databases

Gene3Di2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR015864. FAD_synthase.
IPR023468. Riboflavin_kinase.
IPR002606. Riboflavin_kinase_bac.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR22749. PTHR22749. 1 hit.
PfamiPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFiPIRSF004491. FAD_Synth. 1 hit.
SMARTiSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMiSSF82114. SSF82114. 1 hit.
TIGRFAMsiTIGR00083. ribF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WZW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVSIGVFDG VHIGHQKVLR TMKEIAFFRK DDSLIYTISY PPEYFLPDFP
60 70 80 90 100
GLLMTVESRV EMLSRYARTV VLDFFRIKDL TPEGFVERYL SGVSAVVVGR
110 120 130 140 150
DFRFGKNASG NASFLRKKGV EVYEIEDVVV QGKRVSSSLI RNLVQEGRVE
160 170 180 190 200
EIPAYLGRYF EIEGIVHKDR EFGRKLGFPT ANIDRGNEKL VDLKRGVYLV
210 220 230 240 250
RVHLPDGKKK FGVMNVGFRP TVGDARNVKY EVYILDFEGD LYGQRLKLEV
260 270 280 290
LKFMRDEKKF DSIEELKAAI DQDVKSARNM IDDIINSKFE KEG
Length:293
Mass (Da):33,614
Last modified:November 1, 1999 - v1
Checksum:i42B56B582C03BEB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35939.1.
CP004077 Genomic DNA. Translation: AGL49784.1.
PIRiB72325.
RefSeqiNP_228666.1. NC_000853.1.
WP_004080749.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35939; AAD35939; TM_0857.
AGL49784; AGL49784; Tmari_0859.
GeneIDi898530.
KEGGitma:TM0857.
tmi:THEMA_00350.
tmm:Tmari_0859.
tmw:THMA_0879.
PATRICi23936642. VBITheMar51294_0870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35939.1.
CP004077 Genomic DNA. Translation: AGL49784.1.
PIRiB72325.
RefSeqiNP_228666.1. NC_000853.1.
WP_004080749.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRZX-ray1.90A/B1-293[»]
1S4MX-ray2.10A/B1-293[»]
1T6XX-ray2.29A/B1-293[»]
1T6YX-ray2.80A/B1-293[»]
1T6ZX-ray2.40A/B1-293[»]
2I1LX-ray2.50A/B1-293[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0857.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35939; AAD35939; TM_0857.
AGL49784; AGL49784; Tmari_0859.
GeneIDi898530.
KEGGitma:TM0857.
tmi:THEMA_00350.
tmm:Tmari_0859.
tmw:THMA_0879.
PATRICi23936642. VBITheMar51294_0870.

Phylogenomic databases

eggNOGiENOG4105DTN. Bacteria.
COG0196. LUCA.
KOiK11753.
OMAiFPTANMR.
OrthoDBiEOG6QP0ZV.

Enzyme and pathway databases

UniPathwayiUPA00276; UER00406.
UPA00277; UER00407.
BioCyciTMAR243274:GC6P-887-MONOMER.

Family and domain databases

Gene3Di2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR015864. FAD_synthase.
IPR023468. Riboflavin_kinase.
IPR002606. Riboflavin_kinase_bac.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR22749. PTHR22749. 1 hit.
PfamiPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFiPIRSF004491. FAD_Synth. 1 hit.
SMARTiSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMiSSF82114. SSF82114. 1 hit.
TIGRFAMsiTIGR00083. ribF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099Imported and MSB8Imported.
  2. "Crystal structure of a flavin-binding protein from Thermotoga maritima."
    Wang W., Kim R., Jancarik J., Yokota H., Kim S.H.
    Proteins 52:633-635(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
  3. "Crystal structure of ADP bound FAD synthetase."
    Shin D.H., Wang W., Kim R., Yokota H., Kim S.-H.
    Submitted (MAY-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH ADP; AMP AND FMN.
  4. "Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima."
    Wang W., Kim R., Yokota H., Kim S.H.
    Proteins 58:246-248(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
  5. "Crystal structure of the C2 form of FAD synthetase from Thermotoga maritima."
    Wang W., Shin D.H., Yokota H., Kim R., Kim S.-H.
    Submitted (AUG-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
  6. "The genome organization of Thermotoga maritima reflects its lifestyle."
    Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., Zengler K.
    PLoS Genet. 9:E1003485-E1003485(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099Imported and MSB8Imported.

Entry informationi

Entry nameiQ9WZW1_THEMA
AccessioniPrimary (citable) accession number: Q9WZW1
Secondary accession number(s): G4FCW7
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1999
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.