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Protein

Flavin-dependent thymidylate synthase

Gene

thyX

Organism
Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH2 as the reductant.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP+.UniRule annotation

Cofactori

FADUniRule annotationNote: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.UniRule annotation

Pathwayi: dTTP biosynthesis

This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei71FAD; shared with neighboring subunitsUniRule annotation1
Binding sitei103FAD; shared with neighboring subunitsUniRule annotation1
Binding sitei172dUMPUniRule annotation1
Binding sitei194FADUniRule annotation1
Active sitei199Involved in ionization of N3 of dUMP, leading to its activationUniRule annotation1
Binding sitei199dUMP; shared with dimeric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi92 – 95dUMP; shared with dimeric partnerUniRule annotation4
Nucleotide bindingi95 – 97FADUniRule annotation3
Nucleotide bindingi103 – 107dUMPUniRule annotation5
Nucleotide bindingi188 – 190FAD; shared with neighboring subunitsUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavin-dependent thymidylate synthaseUniRule annotation (EC:2.1.1.148UniRule annotation)
Short name:
FDTSUniRule annotation
Alternative name(s):
FAD-dependent thymidylate synthaseUniRule annotation
Thymidylate synthase ThyXUniRule annotation
Short name:
TSUniRule annotation
Short name:
TSaseUniRule annotation
Gene namesi
Name:thyXUniRule annotation
Ordered Locus Names:Mflv_4001
OrganismiMycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK))
Taxonomic identifieri350054 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000232 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001845921 – 250Flavin-dependent thymidylate synthaseAdd BLAST250

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi350054.Mflv_4001.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 233ThyXUniRule annotationAdd BLAST227

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi95 – 105ThyX motifUniRule annotationAdd BLAST11

Sequence similaritiesi

Belongs to the thymidylate synthase ThyX family.UniRule annotation
Contains 1 thyX (flavin-dependent thymidylate synthase) domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107SMJ. Bacteria.
COG1351. LUCA.
HOGENOMiHOG000047391.
KOiK03465.
OMAiACYQSWN.
OrthoDBiPOG091H0B3V.

Family and domain databases

HAMAPiMF_01408. ThyX. 1 hit.
InterProiIPR003669. Thymidylate_synthase_ThyX.
[Graphical view]
PfamiPF02511. Thy1. 1 hit.
[Graphical view]
SUPFAMiSSF69796. SSF69796. 1 hit.
TIGRFAMsiTIGR02170. thyX. 1 hit.
PROSITEiPS51331. THYX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4TCJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEIAPLRVQ LIAKTEFSAP PDVEWSTDAD GGAALVEFAG RACYQSWSKP
60 70 80 90 100
NPRTATNATY VRHIIDVGHF SVLEHASVSF YITGLSRSCT HELIRHRHFS
110 120 130 140 150
YSQLSQRYVP ENDAEVVAPP GIEDDPELLA LFTAATDASR AAYTELLNRL
160 170 180 190 200
EAKLADQGTS TLRRKQARQA ARAVLPNATE TRIVVTGNYR AWRHFIAMRA
210 220 230 240 250
SEHADVEIRR LAIECLRRLV AVAPQVFSDF EITALADGTE VATSPLATEV
Length:250
Mass (Da):27,604
Last modified:May 15, 2007 - v1
Checksum:iBE6306C7C8A16BFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000656 Genomic DNA. Translation: ABP46472.1.
RefSeqiWP_011894852.1. NC_009338.1.

Genome annotation databases

EnsemblBacteriaiABP46472; ABP46472; Mflv_4001.
KEGGimgi:Mflv_4001.
PATRICi18036205. VBIMycGil17082_4073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000656 Genomic DNA. Translation: ABP46472.1.
RefSeqiWP_011894852.1. NC_009338.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi350054.Mflv_4001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP46472; ABP46472; Mflv_4001.
KEGGimgi:Mflv_4001.
PATRICi18036205. VBIMycGil17082_4073.

Phylogenomic databases

eggNOGiENOG4107SMJ. Bacteria.
COG1351. LUCA.
HOGENOMiHOG000047391.
KOiK03465.
OMAiACYQSWN.
OrthoDBiPOG091H0B3V.

Enzyme and pathway databases

UniPathwayiUPA00575.

Family and domain databases

HAMAPiMF_01408. ThyX. 1 hit.
InterProiIPR003669. Thymidylate_synthase_ThyX.
[Graphical view]
PfamiPF02511. Thy1. 1 hit.
[Graphical view]
SUPFAMiSSF69796. SSF69796. 1 hit.
TIGRFAMsiTIGR02170. thyX. 1 hit.
PROSITEiPS51331. THYX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHYX_MYCGI
AccessioniPrimary (citable) accession number: A4TCJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 15, 2007
Last modified: November 30, 2016
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.