Q9ZMN7 (FABI_HELPJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 81.
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: Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Short name=ENR EC=1.3.1.9 Alternative name(s): NADH-dependent enoyl-ACP reductase | ||||
| Gene names |
| ||||
| Organism | Helicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 85963 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter |
Protein attributes
| Sequence length | 275 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism By similarity. |
| Catalytic activity | Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerizationInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 275 | 275 | Enoyl-[acyl-carrier-protein] reductase [NADH] FabI | PRO_0000054903 | |||||
Regions | |||||||||
| Nucleotide binding | 19 – 20 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 64 – 65 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 191 – 195 | 5 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 145 | 1 | Proton acceptor By similarity | ||||||
| Active site | 155 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 13 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 92 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 95 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 162 | 1 | NAD By similarity | ||||||
| Site | 203 | 1 | Involved in acyl-ACP binding By similarity | ||||||
Sequences
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References
| [1] | "Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. Trust T.J.Nature 397:176-180(1999) [PubMed: 9923682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J99. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE001439 Genomic DNA. Translation: AAD05765.1. |
| PIR | B71964. |
| RefSeq | NP_222902.1. NC_000921.1. |
3D structure databases | |
| ProteinModelPortal | Q9ZMN7. |
| SMR | Q9ZMN7. Positions 2-275. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9ZMN7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 889293. |
| GenomeReviews | Gene locus jhp_0181 in contig AE001439_GR. |
| KEGG | hpj:jhp0181. |
| NMPDR | fig|85963.1.peg.180. |
| PATRIC | 20604984. VBIHelPyl98156_0204. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0623. |
| HOGENOM | HBG750976. |
| OMA | MILKWNE. |
| PhylomeDB | Q9ZMN7. |
| ProtClustDB | PRK08415. |
Enzyme and pathway databases | |
| BioCyc | HPYL85963:JHP0181-MONOMER. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR014358. Enoyl-ACP_Rdtase_NADH. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00208. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PIRSF | PIRSF000094. Enoyl-ACP_rdct. 1 hit. |
| PRINTS | PR00081. GDHRDH. |
| ProtoNet | Search... |
Entry information
| Entry name | FABI_HELPJ | ||||||||
| Accession | Primary (citable) accession number: Q9ZMN7 | ||||||||
| 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 |

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