P72216 (LPXB_PROMI) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 3, 2012.
Version 41.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lipid-A-disaccharide synthase EC=2.4.1.182 | ||
| Gene names |
| ||
| Organism | Proteus mirabilis | ||
| Taxonomic identifier | 584 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus![]() |
Protein attributes
| Sequence length | 141 AA. |
| Sequence status | Fragment. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00392 |
| Catalytic activity | UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. HAMAP-Rule MF_00392 |
| Pathway | Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 5/6. HAMAP-Rule MF_00392 |
| Sequence similarities | Belongs to the LpxB family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid A biosynthesis Lipid biosynthesis Lipid metabolism |
| Molecular function | Glycosyltransferase Transferase |
| Gene Ontology (GO) | |
| Biological_process | lipid A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | lipid-A-disaccharide synthase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›141 | ›141 | Lipid-A-disaccharide synthase HAMAP-Rule MF_00392 | PRO_0000190175 | ||||
Experimental info | ||||||||
| Non-terminal residue | 141 | 1 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | Servos S., Khan S.A., Papakonstantinopoulou A., Dougan G., Maskell D. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PR 990. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y09263 Genomic DNA. Translation: CAA70457.1. |
3D structure databases | |
| ProteinModelPortal | P72216. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GT19. Glycosyltransferase Family 19. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00359; UER00481. |
Family and domain databases | |
| HAMAP | MF_00392. LpxB. |
| InterPro | IPR003835. Glyco_trans_19. [Graphical view] |
| Pfam | PF02684. LpxB. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00215. lpxB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LPXB_PROMI | ||||||||
| Accession | Primary (citable) accession number: P72216 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
