Reviewed,
UniProtKB/Swiss-Prot Q81RW4 (LDH1_BACAN)
Last modified
February 9, 2010.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-lactate dehydrogenase 1 Short name=L-LDH 1 EC=1.1.1.27 | ||||||
| Gene names |
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| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1392 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 314 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | (S)-lactate + NAD+ = pyruvate + NADH. HAMAP MF_00488 |
| Pathway | Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP MF_00488 |
| Subunit structure | Homotetramer By similarity. HAMAP MF_00488 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00488. |
| Sequence similarities | Belongs to the LDH/MDH superfamily. LDH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | anaerobic glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | L-lactate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 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 – 314 | 314 | L-lactate dehydrogenase 1 HAMAP MF_00488 | PRO_0000168313 | |||||
Regions | |||||||||
| Nucleotide binding | 14 – 42 | 29 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 178 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 91 | 1 | Substrate By similarity | ||||||
| Binding site | 123 | 1 | NAD or substrate By similarity | ||||||
| Binding site | 154 | 1 | Substrate By similarity | ||||||
| Binding site | 232 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 223 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP25818.1. AE017334 Genomic DNA. Translation: AAT31043.2. AE017225 Genomic DNA. Translation: AAT54099.1. |
| RefSeq | NP_844332.1. YP_018568.2. YP_028048.1. |
3D structure databases | |
| SMR | Q81RW4. Positions 4-311. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1086286. 2816222. 2850587. |
| GenomeReviews | Gene locus BA_1923 in contig AE016879_GR. Gene locus BAS1784 in contig AE017225_GR. Gene locus GBAA_1923 in contig AE017334_GR. |
| KEGG | ban:BA1923. bar:GBAA1923. bat:BAS1784. |
| TIGR | BA_1923. GBAA_1923. |
Phylogenomic databases | |
| HOGENOM | HBG566126. |
| OMA | KEEHAHA. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS1784-MONOMER. BANT261594:GBAA1923-MONOMER. |
| BRENDA | 1.1.1.27. 267517. |
Family and domain databases | |
| HAMAP | MF_00488. Lactate_dehydrog. [Tree] |
| InterPro | IPR001557. L-lactate/malate_DH. IPR011304. L-lactate_DH. IPR018177. L-lactate_DH_AS. IPR001236. Lactate/malate_DH. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| PRINTS | PR00086. LLDHDRGNASE. |
| TIGRFAMs | TIGR01771. L-LDH-NAD. 1 hit. |
| PROSITE | PS00064. L_LDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LDH1_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81RW4 Secondary accession number(s): Q6I040, Q6KU19 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


