Q1LU65 (PLSB_BAUCH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 38.
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: Glycerol-3-phosphate acyltransferase Short name=GPAT EC=2.3.1.15 | ||||
| Gene names |
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| Organism | Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 374463 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia |
Protein attributes
| Sequence length | 821 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393 |
| Pathway | Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393 |
| Subcellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_00393. |
| Domain | The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity. HAMAP MF_00393 |
| Sequence similarities | Belongs to the GPAT/DAPAT family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phospholipid biosynthesis |
| Cellular component | Cell membrane Membrane |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | glycerol-3-phosphate O-acyltransferase 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 – 821 | 821 | Glycerol-3-phosphate acyltransferase HAMAP MF_00393 | PRO_1000049428 | |||||
Regions | |||||||||
| Motif | 310 – 315 | 6 | HXXXXD motif HAMAP MF_00393 | ||||||
Sequences
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References
| [1] | "Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000238 Genomic DNA. Translation: ABF13834.1. |
| RefSeq | YP_588499.1. NC_007984.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1LU65. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4056612. |
| GenomeReviews | Gene locus BCI_0020 in contig CP000238_GR. |
| KEGG | bci:BCI_0020. |
| PATRIC | 21073527. VBIBauCic75062_0020. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2937. |
| HOGENOM | HBG296590. |
| OMA | WNKLYQG. |
Enzyme and pathway databases | |
| BioCyc | BCIC186490:BCI_0020-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00393. Glyc3P_acyltrans. [Tree] |
| InterPro | IPR002123. Acyltransferase. IPR022284. G3P_O-AcylTrfase. [Graphical view] |
| KO | K00631. |
| Pfam | PF01553. Acyltransferase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000437. GPAT_DHAPAT. 1 hit. |
| SMART | SM00563. PlsC. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03703. PlsB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PLSB_BAUCH | ||||||||
| Accession | Primary (citable) accession number: Q1LU65 | ||||||||
| Entry history |
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| 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 |

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