Reviewed, UniProtKB/Swiss-Prot Q5B998 (DHOM_EMENI)

Names and origin

Protein names

Recommended name:
    Homoserine dehydrogenase
      Short name=HDH
    EC=1.1.1.3

Gene names

ORF Names:

AN2882

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in osmoadaptation.
Catalytic activity	L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
Induction	Down-regulated when grown with elevated levels of potassium chloride. Ref.2
Sequence similarities	Belongs to the homoserine dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis Methionine biosynthesis Stress response Threonine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro homoserine dehydrogenase 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 – 368	368	Homoserine dehydrogenase		PRO_0000348284
Regions
	Nucleotide binding	10 – 17	8	NADP By similarity
Sites
	Active site	227	1	Proton donor Potential
	Binding site	95	1	NADP By similarity
	Binding site	119	1	NADP By similarity
	Binding site	212	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5B998-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 487985B2CF176A79	FASTA	368	38,652
	10 20 30 40 50 60 MSAPIYLGVI GVGGVGTAFL NQLARLPNAP KLILLARSSQ TLLSPTPSYS PTIPAAEWKT 70 80 90 100 110 120 AVETPSLTKS GALTPDEIAT YLASAPGRSI LVDNTSDPAL ASNYPVFLRK GISVVTPNKK 130 140 150 160 170 180 GFSSDLSLWK EIFAAAAEGK ALVYHESTVG AGLPVISTLK DLVNTGDEVT RIEGVFSGTL 190 200 210 220 230 240 SFLFNTFAPA SGSSSAKWSE VVSQAKELGY TEPDPRDDLN GMDVARKLTI LARIAGLDVQ 250 260 270 280 290 300 SPDSFPIESL IPAELTSLPS SADGIAQFMA RLPEFDSQMA AIKEGAEKAG KVVRYVGSVD 310 320 330 340 350 360 VAKKEVRVGL QQFDKDSAIA GLKGSDNIIS FYTRRYGSNP LIVQGAGAGG DVTAMGVTAD LLKVIERL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.
[2]	"Proteome map of Aspergillus nidulans during osmoadaptation." Kim Y., Nandakumar M.P., Marten M.R. Fungal Genet. Biol. 44:886-895(2007) [PubMed: 17258477] [Abstract] Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACD01000051 Genomic DNA. Translation: EAA63453.1.
RefSeq	XP_660486.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2873909.
KEGG	ani:AN2882.2.
Family and domain databases
InterPro	IPR005106. Asp/hSer_DH_NAD-bd. IPR001342. Homoserine_dehydrogenase_cat. IPR019811. Homoserine_dehydrogenase_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PROSITE	PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHOM_EMENI

Accession

Primary (citable) accession number: Q5B998

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	April 26, 2005
Last modified:	June 16, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)