A1KRL1 (FABZ_NEIMF) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 44.
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: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ EC=4.2.1.59 Alternative name(s): (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase Short name=(3R)-hydroxymyristoyl-ACP dehydrase Beta-hydroxyacyl-ACP dehydratase | ||||
| Gene names |
| ||||
| Organism | Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / FAM18) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272831 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › ![]() |
Protein attributes
| Sequence length | 149 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs By similarity. HAMAP-Rule MF_00406 |
| Catalytic activity | A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O. HAMAP-Rule MF_00406 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the thioester dehydratase family. FabZ subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid A biosynthesis Lipid biosynthesis Lipid metabolism |
| Cellular component | Cytoplasm |
| Molecular function | Lyase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP lipid A biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase 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 – 149 | 149 | 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ HAMAP-Rule MF_00406 | PRO_0000301905 | |||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||
| Active site | 53 | 1 | By similarity | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Beta strand | 5 – 8 | 4 | |||||||||||||||||||||||||||||||
| Helix | 9 – 15 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 27 – 32 | 6 | |||||||||||||||||||||||||||||||
| Turn | 33 – 35 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 36 – 42 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 45 – 47 | 3 | |||||||||||||||||||||||||||||||
| Helix | 48 – 51 | 4 | |||||||||||||||||||||||||||||||
| Helix | 62 – 80 | 19 | |||||||||||||||||||||||||||||||
| Turn | 85 – 87 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 91 – 95 | 5 | |||||||||||||||||||||||||||||||
| Beta strand | 97 – 100 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 109 – 120 | 12 | |||||||||||||||||||||||||||||||
| Beta strand | 123 – 132 | 10 | |||||||||||||||||||||||||||||||
| Beta strand | 135 – 145 | 11 | |||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18." Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. Parkhill J.PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700532 / FAM18. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AM421808 Genomic DNA. Translation: CAM09489.1. | ||||||||||||
| RefSeq | YP_974299.1. NC_008767.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | A1KRL1. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 272831.NMC0170. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | CAM09489; CAM09489; NMC0170. | ||||||||||||
| GeneID | 4675013. | ||||||||||||
| KEGG | nmc:NMC0170. | ||||||||||||
| PATRIC | 20349847. VBINeiMen17609_0188. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0764. | ||||||||||||
| HOGENOM | HOG000277829. | ||||||||||||
| KO | K02372. | ||||||||||||
| OMA | CETELMF. | ||||||||||||
| ProtClustDB | PRK00006. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | NMEN272831:GJDX-172-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00406. FabZ. | ||||||||||||
| InterPro | IPR013114. FabA_FabZ. IPR010084. FabZ. [Graphical view] | ||||||||||||
| Pfam | PF07977. FabA. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR01750. fabZ. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | FABZ_NEIMF | ||||||||
| Accession | Primary (citable) accession number: A1KRL1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
