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Protein

dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose transaminase

Gene

desV

Organism
Streptomyces venezuelae
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of dTDP-alpha-D-desosamine, a sugar found in several bacterial macrolide antibiotics. Catalyzes the reversible transfer of the amino group from L-glutamate to the C-3 position of dTDP-3-keto-4,6-deoxyglucose to yield dTDP-3-amino-3,4,6-trideoxyglucose.1 Publication

Catalytic activityi

dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose + 2-oxoglutarate = dTDP-3-dehydro-4,6-deoxy-alpha-D-glucose + L-glutamate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi: Antibiotic biosynthesis

This protein is involved in Antibiotic biosynthesis.Curated
View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei67Pyridoxal phosphate; via amide nitrogen1 Publication1
Binding sitei167Pyridoxal phosphate1 Publication1
Binding sitei221Pyridoxal phosphate1 Publication1
Binding sitei227Pyridoxal phosphate1 Publication1
Binding sitei318Pyridoxal phosphate1 Publication1

GO - Molecular functioni

  • pyridoxal phosphate binding Source: UniProtKB
  • transaminase activity Source: UniProtKB

GO - Biological processi

  • macrolide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16953.
BRENDAi2.6.1.106. 6106.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose transaminase1 Publication (EC:2.6.1.1061 Publication)
Gene namesi
Name:desV1 Publication
OrganismiStreptomyces venezuelae
Taxonomic identifieri54571 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004308321 – 379dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose transaminaseAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei193N6-(pyridoxal phosphate)lysine1 Publication1

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 21Combined sources7
Helixi23 – 36Combined sources14
Beta strandi40 – 42Combined sources3
Helixi43 – 55Combined sources13
Beta strandi58 – 65Combined sources8
Helixi67 – 77Combined sources11
Beta strandi85 – 92Combined sources8
Helixi95 – 102Combined sources8
Beta strandi106 – 110Combined sources5
Beta strandi114 – 119Combined sources6
Helixi121 – 127Combined sources7
Beta strandi132 – 135Combined sources4
Helixi140 – 142Combined sources3
Helixi147 – 157Combined sources11
Beta strandi160 – 164Combined sources5
Beta strandi184 – 188Combined sources5
Beta strandi193 – 195Combined sources3
Beta strandi202 – 207Combined sources6
Helixi209 – 219Combined sources11
Helixi240 – 251Combined sources12
Helixi253 – 270Combined sources18
Turni271 – 273Combined sources3
Beta strandi291 – 296Combined sources6
Helixi300 – 309Combined sources10
Helixi322 – 324Combined sources3
Helixi326 – 329Combined sources4
Helixi339 – 347Combined sources9
Beta strandi348 – 351Combined sources4
Helixi359 – 374Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OGAX-ray2.05A/B/C/D1-379[»]
2OGEX-ray2.05A/B/C/D1-379[»]
ProteinModelPortaliQ9ZGH4.
SMRiQ9ZGH4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZGH4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni188 – 193Pyridoxal phosphate binding1 Publication6
Regioni235 – 237Pyridoxal phosphate binding1 Publication3

Sequence similaritiesi

Belongs to the degT/dnrJ/eryC1 family.Curated

Phylogenomic databases

KOiK13310.

Family and domain databases

CDDicd00616. AHBA_syn. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9ZGH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRAETPRV PFLDLKAAYE ELRAETDAAI ARVLDSGRYL LGPELEGFEA
60 70 80 90 100
EFAAYCETDH AVGVNSGMDA LQLALRGLGI GPGDEVIVPS HTYIASWLAV
110 120 130 140 150
SATGATPVPV EPHEDHPTLD PLLVEKAITP RTRALLPVHL YGHPADMDAL
160 170 180 190 200
RELADRHGLH IVEDAAQAHG ARYRGRRIGA GSSVAAFSFY PGKNLGCFGD
210 220 230 240 250
GGAVVTGDPE LAERLRMLRN YGSRQKYSHE TKGTNSRLDE MQAAVLRIRL
260 270 280 290 300
AHLDSWNGRR SALAAEYLSG LAGLPGIGLP VTAPDTDPVW HLFTVRTERR
310 320 330 340 350
DELRSHLDAR GIDTLTHYPV PVHLSPAYAG EAPPEGSLPR AESFARQVLS
360 370
LPIGPHLERP QALRVIDAVR EWAERVDQA
Length:379
Mass (Da):41,184
Last modified:May 1, 1999 - v1
Checksum:i1A4FD0F4E76DCCDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079762 Genomic DNA. Translation: AAC68680.1.
RefSeqiWP_055641633.1. NZ_LN881739.1.

Genome annotation databases

KEGGiag:AAC68680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079762 Genomic DNA. Translation: AAC68680.1.
RefSeqiWP_055641633.1. NZ_LN881739.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OGAX-ray2.05A/B/C/D1-379[»]
2OGEX-ray2.05A/B/C/D1-379[»]
ProteinModelPortaliQ9ZGH4.
SMRiQ9ZGH4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC68680.

Phylogenomic databases

KOiK13310.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16953.
BRENDAi2.6.1.106. 6106.

Miscellaneous databases

EvolutionaryTraceiQ9ZGH4.

Family and domain databases

CDDicd00616. AHBA_syn. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDESV_STRVZ
AccessioniPrimary (citable) accession number: Q9ZGH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 64 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

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.