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UniProtKB - Q9S5E2 (DOIS_NIACI)
Protein
2-deoxy-scyllo-inosose synthase
Gene
btrC
Organism
Niallia circulans (Bacillus circulans)
Status
Functioni
Catalyzes the intramolecular carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI).
Catalytic activityi
- EC:4.2.3.1243 Publications
Cofactori
Protein has several cofactor binding sites:Activity regulationi
Strongly inhibited by EDTA, zinc and Cu2+.
Kineticsi
- KM=900 µM for glucose-6-phosphate (at pH 7.7 and 46 degrees Celsius)1 Publication
- KM=170 µM for NAD+ (at pH 7.7 and 46 degrees Celsius)1 Publication
pH dependencei
Optimum pH is 7.5-8.5.1 Publication
Temperature dependencei
Optimum temperature is 46 degrees Celsius.1 Publication
: 2-deoxystreptamine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 2-deoxystreptamine from D-glucose 6-phosphate. This subpathway is part of the pathway 2-deoxystreptamine biosynthesis, which is itself part of Metabolic intermediate biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-deoxystreptamine from D-glucose 6-phosphate, the pathway 2-deoxystreptamine biosynthesis and in Metabolic intermediate biosynthesis.
Pathwayi: butirosin biosynthesis
This protein is involved in the pathway butirosin biosynthesis, which is part of Antibiotic biosynthesis.View all proteins of this organism that are known to be involved in the pathway butirosin biosynthesis and in Antibiotic biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 42 | NAD1 Publication | 1 | |
Active sitei | 141 | 1 Publication | 1 | |
Binding sitei | 176 | NAD1 Publication | 1 | |
Metal bindingi | 183 | Cobalt1 Publication | 1 | |
Active sitei | 243 | 1 Publication | 1 | |
Metal bindingi | 246 | Cobalt1 Publication | 1 | |
Metal bindingi | 262 | Cobalt1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 72 – 75 | NAD1 Publication | 4 | |
Nucleotide bindingi | 104 – 108 | NAD1 Publication | 5 | |
Nucleotide bindingi | 128 – 129 | NAD1 Publication | 2 | |
Nucleotide bindingi | 139 – 141 | NAD1 Publication | 3 | |
Nucleotide bindingi | 150 – 151 | NAD1 Publication | 2 |
GO - Molecular functioni
- carbon-oxygen lyase activity, acting on phosphates Source: InterPro
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- antibiotic biosynthetic process Source: UniProtKB-KW
- aromatic amino acid family biosynthetic process Source: InterPro
Keywordsi
Molecular function | Lyase |
Biological process | Antibiotic biosynthesis |
Ligand | Cobalt, Metal-binding, NAD |
Enzyme and pathway databases
BRENDAi | 4.2.3.124, 649 |
SABIO-RKi | Q9S5E2 |
UniPathwayi | UPA00907;UER00921 UPA00964 |
Names & Taxonomyi
Protein namesi | Recommended name: 2-deoxy-scyllo-inosose synthase (EC:4.2.3.124)Short name: DOI synthase Short name: DOIS |
Gene namesi | Name:btrC |
Organismi | Niallia circulans (Bacillus circulans) |
Taxonomic identifieri | 1397 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Niallia |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000234034 | 1 – 368 | 2-deoxy-scyllo-inosose synthaseAdd BLAST | 368 |
Interactioni
Subunit structurei
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9S5E2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9S5E2 |
Family & Domainsi
Sequence similaritiesi
Family and domain databases
InterProi | View protein in InterPro IPR030963, DHQ_synth_fam IPR030960, DHQS/DOIS |
Pfami | View protein in Pfam PF01761, DHQ_synthase, 1 hit |
PIRSFi | PIRSF001455, DHQ_synth, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9S5E2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTTKQICFAD RCFNFAFGEH VLESVESYIP RDEFDQYIMI SDSGVPDSIV
60 70 80 90 100
HYAAEYFGKL APVHILRFQG GEEYKTLSTV TNLQERAIAL GANRRTAIVA
110 120 130 140 150
VGGGLTGNVA GVAAGMMFRG IALIHVPTTF LAASDSVLSI KQAVNLTSGK
160 170 180 190 200
NLVGFYYPPR FVFADTRILS ESPPRQVKAG MCELVKNMLI LENDNKEFTE
210 220 230 240 250
DDLNSANVYS PKQLETFINF CISAKMSVLS EDIYEKKKGL IFEYGHTIGH
260 270 280 290 300
AIELAEQGGI THGEAIAVGM IYAAKIANRM NLMPEHDVSA HYWLLNKIGA
310 320 330 340 350
LQDIPLKSDP DSIFHYLIHD NKRGYIKLDE DNLGMILLSG VGKPAMYNQT
360
LLTPVRKTLI KEVIREGL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB019237 Genomic DNA Translation: BAA83344.1 AJ781030 Genomic DNA Translation: CAG77421.1 AB097196 Genomic DNA Translation: BAE07067.1 |
Genome annotation databases
KEGGi | ag:BAE07067 ag:BAE07068 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB019237 Genomic DNA Translation: BAA83344.1 AJ781030 Genomic DNA Translation: CAG77421.1 AB097196 Genomic DNA Translation: BAE07067.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2D2X | X-ray | 2.30 | A/B | 1-368 | [»] | |
2GRU | X-ray | 2.15 | A/B | 1-368 | [»] | |
SMRi | Q9S5E2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Genome annotation databases
KEGGi | ag:BAE07067 ag:BAE07068 |
Enzyme and pathway databases
UniPathwayi | UPA00907;UER00921 UPA00964 |
BRENDAi | 4.2.3.124, 649 |
SABIO-RKi | Q9S5E2 |
Miscellaneous databases
EvolutionaryTracei | Q9S5E2 |
Family and domain databases
InterProi | View protein in InterPro IPR030963, DHQ_synth_fam IPR030960, DHQS/DOIS |
Pfami | View protein in Pfam PF01761, DHQ_synthase, 1 hit |
PIRSFi | PIRSF001455, DHQ_synth, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DOIS_NIACI | |
Accessioni | Q9S5E2Primary (citable) accession number: Q9S5E2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 2, 2006 |
Last sequence update: | May 1, 2000 | |
Last modified: | February 23, 2022 | |
This is version 87 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families