Q05069 (FABI_NOSS1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 79.
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 | Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 103690 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc |
Protein attributes
| Sequence length | 258 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. |
| Sequence caution | The sequence AAD04184.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB76090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
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 – 258 | 258 | Enoyl-[acyl-carrier-protein] reductase [NADH] FabI | PRO_0000054893 | |||||
Regions | |||||||||
| Nucleotide binding | 19 – 20 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 67 – 68 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 194 – 198 | 5 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 148 | 1 | Proton acceptor By similarity | ||||||
| Active site | 158 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 13 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 95 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 98 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 165 | 1 | NAD By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Anabaena sp. strain PCC 7120 bifA gene encoding a sequence-specific DNA-binding protein cloned by in vivo transcriptional interference selection." Wei T.-F., Ramasubramanian T.S., Pu F., Golden J.W. J. Bacteriol. 175:4025-4035(1993) [PubMed: 8391534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. Tabata S.DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7120 / UTEX 2576. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L10036 Genomic DNA. Translation: AAD04184.1. Different initiation. BA000019 Genomic DNA. Translation: BAB76090.1. Different initiation. |
| PIR | AG2354. |
| RefSeq | NP_488431.1. NC_003272.1. |
3D structure databases | |
| ProteinModelPortal | Q05069. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q05069. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1107992. |
| GenomeReviews | Gene locus all4391 in contig BA000019_GR. |
| KEGG | ana:all4391. |
| PATRIC | 22779366. VBINosSp37423_5130. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0623. |
| HOGENOM | HBG750976. |
| OMA | MGVANNR. |
| PhylomeDB | Q05069. |
| ProtClustDB | PRK07370. |
Enzyme and pathway databases | |
| BioCyc | NSP103690:ALL4391-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_NOSS1 | ||||||||
| Accession | Primary (citable) accession number: Q05069 | ||||||||
| 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