Aspartate-semialdehyde dehydrogenase - Haemophilus influenzae

Names and origin

Protein names

Recommended name:
    Aspartate-semialdehyde dehydrogenase
      Short name=ASA dehydrogenase
      Short name=ASADH
    EC=1.2.1.11

Gene names

Name:	asd
Ordered Locus Names:	HI0646

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP⁺ = L-4-aspartyl phosphate + NADPH.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 371

371

Aspartate-semialdehyde dehydrogenase

PRO_0000141375

Sites

Active site

136

1

Acyl-thioester intermediate By similarity

Secondary structure

1

.

371

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P44801-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E44CE5B90F2AF041
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FASTA

371

40,539

        10         20         30         40         50         60 
MKNVGFIGWR GMVGSVLMDR MSQENDFENL NPVFFTTSQA GQKAPVFGGK DAGDLKSAFD 

        70         80         90        100        110        120 
IEELKKLDII VTCQGGDYTN EVYPKLKATG WDGYWVDAAS ALRMKDDAII VLDPVNQHVI 

       130        140        150        160        170        180 
SEGLKKGIKT FVGGNCTVSL MLMAIGGLFE KDLVEWISVA TYQAASGAGA KNMRELLSQM 

       190        200        210        220        230        240 
GLLEQAVSSE LKDPASSILD IERKVTAKMR ADNFPTDNFG AALGGSLIPW IDKLLPETGQ 

       250        260        270        280        290        300 
TKEEWKGYAE TNKILGLSDN PIPVDGLCVR IGALRCHSQA FTIKLKKDLP LEEIEQIIAS 

       310        320        330        340        350        360 
HNEWVKVIPN DKEITLRELT PAKVTGTLSV PVGRLRKLAM GPEYLAAFTV GDQLLWGAAE 

       370 
PVRRILKQLV A

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References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I.

Venter J.C.
Science 269:496-512(1995) [PubMed: 7542800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

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Cross-references

Sequence databases

L42023 Genomic DNA. Translation: AAC22306.1.

PIR

B64084.

RefSeq

NP_438806.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NWC	X-ray	2.04	A/B	1-371	[»]
1NWH	X-ray	2.00	A/B	1-371	[»]
1NX6	X-ray	2.15	A	1-371	[»]
1OZA	X-ray	2.06	A	1-371	[»]
1PQP	X-ray	2.06	A	1-371	[»]
1PQU	X-ray	1.92	A/B/C/D	1-371	[»]
1PR3	X-ray	2.15	A	1-371	[»]
1PS8	X-ray	2.40	A	1-371	[»]
1PU2	X-ray	2.06	A	1-371	[»]
1Q2X	X-ray	2.05	A/B	1-371	[»]
1TA4	X-ray	2.28	A	1-368	[»]
1TB4	X-ray	2.15	A	1-368	[»]

ModBase

Search...

Genome annotation databases

GeneID

949960.

GenomeReviews

Gene locus HI0646 in contig L42023_GR.

KEGG

hin:HI0646.

NMPDR

fig|71421.1.peg.616.

TIGR

HI0646.

Phylogenomic databases

HOGENOM

P44801.

OMA

P44801. IDGLCVR.

Enzyme and pathway databases

BioCyc

HINF71421:HI_0646-MON.

BRENDA

1.2.1.11. 109.

Family and domain databases

InterPro

IPR000319. Asp-semialdehyde_DH_CS.
IPR011534. Asp_ADH_proteob.
IPR012080. Asp_semialdehyde_DH.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_C.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]

PIRSF

PIRSF000148. ASA_dh. 1 hit.

TIGRFAMs

TIGR01745. asd_gamma. 1 hit.

PROSITE

PS01103. ASD. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

DHAS_HAEIN

Accession

Primary (citable) accession number: P44801

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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