1-deoxy-D-xylulose-5-phosphate synthase - Brucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94)

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C9TTT1 (C9TTT1_BRUPB) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 22. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
1-deoxy-D-xylulose-5-phosphate synthase HAMAP-Rule MF_00315
EC=2.2.1.7 HAMAP-Rule MF_00315

Alternative name(s):
1-deoxyxylulose-5-phosphate synthase HAMAP-Rule MF_00315

Gene names

Name:	dxs HAMAP-Rule MF_00315 EMBL AEK53773.1
ORF Names:	BAHG_00761 EMBL EEX99831.1, BPI_I466 EMBL AEK53773.1

Organism

Brucella pinnipedialis (strain NCTC 12890 / BCCN 94-73 / B2/94) [Complete proteome] [HAMAP] EMBL EEX99831.1

Taxonomic identifier

520461 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella ›

Protein attributes

Sequence length	643 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP) By similarity. SAAS SAAS005474 HAMAP-Rule MF_00315
Catalytic activity	Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO₂. SAAS SAAS005474 HAMAP-Rule MF_00315
Cofactor	Binds 1 magnesium ion per subunit By similarity. SAAS SAAS005474 HAMAP-Rule MF_00315 Binds 1 thiamine pyrophosphate per subunit By similarity. SAAS SAAS005474 HAMAP-Rule MF_00315
Pathway	Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1. SAAS SAAS005474 HAMAP-Rule MF_00315
Subunit structure	Homodimer By similarity. SAAS SAAS005474 HAMAP-Rule MF_00315
Sequence similarities	Belongs to the transketolase family. DXPS subfamily. HAMAP-Rule MF_00315

Ontologies

Keywords
Biological process	Isoprene biosynthesis SAAS SAAS005474 HAMAP-Rule MF_00315 Thiamine biosynthesis SAAS SAAS005474 HAMAP-Rule MF_00315
Ligand	Magnesium SAAS SAAS005474 HAMAP-Rule MF_00315 Metal-binding SAAS SAAS005474 HAMAP-Rule MF_00315 Thiamine pyrophosphate SAAS SAAS005474 HAMAP-Rule MF_00315
Molecular function	Transferase SAAS SAAS005474 HAMAP-Rule MF_00315
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	1-deoxy-D-xylulose 5-phosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway terpenoid biosynthetic process Inferred from electronic annotation. Source: HAMAP thiamine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	1-deoxy-D-xylulose-5-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP thiamine pyrophosphate binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

119 – 121

Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315

Region

151 – 152

Thiamine pyrophosphate binding By similarity HAMAP-Rule MF_00315

Sites

Metal binding

150

Magnesium By similarity HAMAP-Rule MF_00315

Metal binding

179

Magnesium By similarity HAMAP-Rule MF_00315

Binding site

Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Binding site

179

Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Binding site

288

Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Binding site

370

Thiamine pyrophosphate By similarity HAMAP-Rule MF_00315

Sequences

Sequence

Length

Mass (Da)

Tools

C9TTT1 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: 4948F8DD11A59F65
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FASTA

643

69,153

        10         20         30         40         50         60 
MSRPSTPLLD KAPTPDRLRA LPEQDLPQLA EELRTELIDA VSTTGGHLGA GLGVVELTVA 

        70         80         90        100        110        120 
LHHVFNTPYD RIIWDVGHQA YPHKILTGRR DRIRTLRQAG GLSGFTKRAE SEYDPFGAAH 

       130        140        150        160        170        180 
SSTSISAGLG MAVASELSGE KRNVIAVIGD GSMSAGMAYE AMNNAGALDA RLIVILNDND 

       190        200        210        220        230        240 
MSIAPPTGAM SAYLARLVSG RTYRSVREAA KQVAQKLPKF LQDKARKSEE YARAFFTGGT 

       250        260        270        280        290        300 
LFEELGFYYV GPIDGHNLDH LLPVLKNVRD TQKGPVLIHV VTQKGKGYAP AEAAADKYHG 

       310        320        330        340        350        360 
VNEFDVITGK QAKPPANAPS YTKIFGTSLI EEARHDDKIV AVTAAMPTGT GLDLFGEAFP 

       370        380        390        400        410        420 
KRVFDVGIAE QHAVTFAAGL ASEGYKPFCA IYSTFLQRGY DQVVHDVSIQ NLPVRFPIDR 

       430        440        450        460        470        480 
AGLVGADGPT HAGSFDTGFL AALPGFVVMA ASDEAELRHM VRTAAEYDEG PISFRYPRGD 

       490        500        510        520        530        540 
GVGVDLPERG SVLEIGKGRI VREGTKVALL SFGTRLQECL AAAEELGAAG LSTTVADARF 

       550        560        570        580        590        600 
AKPLDHDLIR RLAREHEVLV MVEEGAVGGF GSHVLQFLAT DGLLDRGLKV RALTLPDIYQ 

       610        620        630        640 
DHGKPDAMYA EAGLDRTGIV RTVFAALHRD ELGHEALPTP FRA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Genome Sequence of Brucella pinnipedialis B2/94." The Broad Institute Genome Sequencing Platform Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C. Birren B. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: B2/94 EMBL EEX99831.1.
[2]	Zygmunt M., Clockaert A. Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: B2/94 EMBL AEK53773.1.
[3]	"The genome sequence of Brucella pinnipedialis B2/94 sheds light on the evolutionary history of the genus Brucella." Audic S., Lescot M., Claverie J.M., Cloeckaert A., Zygmunt M.S. BMC Evol. Biol. 11:200-200(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B2/94 EMBL AEK53773.1 and NCTC 12890 / BCCN 94-73 / B2/94.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002078 Genomic DNA. Translation: AEK53773.1. DS999848 Genomic DNA. Translation: EEX99831.1.
RefSeq	YP_004755541.1. NC_015857.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEK53773; AEK53773; BPI_I466. EEX99831; EEX99831; BAHG_00761.
GeneID	10996945.
KEGG	bpp:BPI_I466.
PATRIC	24250790. VBIBruPin17457_0401.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K01662.
Enzyme and pathway databases
BioCyc	BPIN520461:GJF0-465-MONOMER.
UniPathway	UPA00064; UER00091.
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
HAMAP	MF_00315. DXP_synth.
InterPro	IPR005477. Dxylulose-5-P_synthase. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR020826. Transketolase_BS. IPR005476. Transketolase_C. IPR005474. Transketolase_N. [Graphical view]
Pfam	PF13292. DXP_synthase_N. 1 hit. PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
TIGRFAMs	TIGR00204. dxs. 1 hit.
PROSITE	PS00801. TRANSKETOLASE_1. 1 hit. PS00802. TRANSKETOLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C9TTT1_BRUPB

Accession

Primary (citable) accession number: C9TTT1

Entry history

Integrated into UniProtKB/TrEMBL:	November 24, 2009
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information