Reviewed,
UniProtKB/Swiss-Prot P00365 (DHE2_NEUCR)
Last modified
January 19, 2010.
Version 76.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: NAD-specific glutamate dehydrogenase Short name=NAD-GDH EC=1.4.1.2 | ||||
| Gene names |
| ||||
| Organism | Neurospora crassa [Complete proteome] | ||||
| Taxonomic identifier | 5141 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora |
Protein attributes
| Sequence length | 1050 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH. |
| Subunit structure | Homotetramer. |
| Sequence similarities | Belongs to the Glu/Leu/Phe/Val dehydrogenases family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | glutamate catabolic process to 2-oxoglutarate Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro glutamate dehydrogenase activityInferred 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 – 1050 | 1050 | NAD-specific glutamate dehydrogenase | PRO_0000182732 | |||||
Sites | |||||||||
| Active site | 594 | 1 | By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 3 – 5 | 3 | SPS → APD AA sequence Ref.3 | ||||||
| Sequence conflict | 11 | 1 | H → R AA sequence Ref.3 | ||||||
| Sequence conflict | 31 – 41 | 11 | HVSYPKVNGNG → VPYSKVDGGN AA sequence Ref.3 | ||||||
| Sequence conflict | 44 | 1 | V → Q AA sequence Ref.3 | ||||||
| Sequence conflict | 113 – 114 | 2 | TS → ST AA sequence Ref.3 | ||||||
| Sequence conflict | 153 | 1 | T → TTN AA sequence Ref.3 | ||||||
| Sequence conflict | 154 | 1 | Missing in AAB28355. Ref.1 | ||||||
| Sequence conflict | 216 | 1 | P → PEGDP AA sequence Ref.3 | ||||||
| Sequence conflict | 345 – 347 | 3 | LPQ → PQL AA sequence Ref.3 | ||||||
| Sequence conflict | 351 – 352 | 2 | HN → NH AA sequence Ref.3 | ||||||
| Sequence conflict | 461 – 464 | 4 | EVLS → SEVL AA sequence Ref.4 | ||||||
| Sequence conflict | 637 | 1 | L → V in AAB28355. Ref.1 | ||||||
| Sequence conflict | 660 | 1 | T → I in AAB28355. Ref.1 | ||||||
| Sequence conflict | 708 – 709 | 2 | Missing in AAB28355. Ref.1 | ||||||
| Sequence conflict | 753 | 1 | N → D AA sequence Ref.4 | ||||||
| Sequence conflict | 788 | 1 | D → N in AAA33601. Ref.5 | ||||||
| Sequence conflict | 799 – 801 | 3 | VVH → HV AA sequence Ref.4 | ||||||
| Sequence conflict | 845 – 846 | 2 | ST → TS AA sequence Ref.4 | ||||||
| Sequence conflict | 909 | 1 | D → N AA sequence Ref.4 | ||||||
| Sequence conflict | 1024 | 1 | V → VE AA sequence Ref.4 | ||||||
| Sequence conflict | 1035 | 1 | Missing AA sequence Ref.4 | ||||||
| Sequence conflict | 1038 – 1039 | 2 | DF → AD AA sequence Ref.4 | ||||||
| Sequence conflict | 1041 | 1 | S → T in AAB28355. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "NAD(+)-specific glutamate dehydrogenase of Neurospora crassa: cloning, complete nucleotide sequence, and gene mapping." Kapoor M., Vijayaraghavan Y., Kadonaga R., LaRue K.E. Biochem. Cell Biol. 71:205-219(1993) [PubMed: 8398079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. Birren B.W.Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987. |
| [3] | "Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora crassa. Isolation and sequences of several cyanogen bromide peptides from the NH2-terminal portion of the peptide chain." Haberland M.E., Smith E.L. J. Biol. Chem. 255:7984-7992(1980) [PubMed: 6447150] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-44 AND 47-353. |
| [4] | "Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora. IV. The COOH-terminal 669 residues of the peptide chain; comparison with other glutamate dehydrogenases." Austen B.M., Haberland M.E., Nyc J.F., Smith E.L. J. Biol. Chem. 252:8142-8149(1977) [PubMed: 21191] [Abstract] Cited for: PROTEIN SEQUENCE OF 381-1050. |
| [5] | "NAD-specific glutamate dehydrogenase of Neurospora crassa. cDNA cloning and gene expression during derepression." Vierula P.J., Kapoor M. J. Biol. Chem. 264:1108-1114(1989) [PubMed: 2521336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 642-948. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | S66039 Genomic DNA. Translation: AAB28355.1. AABX02000001 Genomic DNA. Translation: EAA27544.1. M23436 mRNA. Translation: AAA33601.1. |
| PIR | DENCED. A92284. T46599. |
| RefSeq | XP_956780.1. |
3D structure databases | |
| SMR | P00365. Positions 479-975. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P00365. |
Genome annotation databases | |
| GeneID | 3872927. |
| KEGG | ncr:NCU00461. |
| NMPDR | fig|5141.1.peg.480. |
Phylogenomic databases | |
| eggNOG | fuNOG04119. |
| OrthoDB | EOG925798. |
| PhylomeDB | P00365. |
Enzyme and pathway databases | |
| BRENDA | 1.4.1.2. 266. |
Family and domain databases | |
| InterPro | IPR006095. Glu/Leu/Phe/Val_DH. IPR006096. Glu/Leu/Phe/Val_DH_C. IPR016210. Glu_DH_NAD-dep. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00208. ELFV_dehydrog. 1 hit. [Graphical view] |
| PIRSF | PIRSF000184. GDH_NAD. 1 hit. |
| SMART | SM00839. ELFV_dehydrog. 1 hit. [Graphical view] |
| PROSITE | PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHE2_NEUCR | ||||||||
| Accession | Primary (citable) accession number: P00365 Secondary accession number(s): Q02222, Q7RUZ7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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