Aspartate-semialdehyde dehydrogenase - Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)

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P41394 (DHAS_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase

Gene names

Name:	asd
Ordered Locus Names:	LB_355

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]

Taxonomic identifier

189518 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira ›

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate By similarity. HAMAP-Rule MF_02121
Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP⁺ = L-4-aspartyl phosphate + NADPH. HAMAP-Rule MF_02121
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. HAMAP-Rule MF_02121 Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. HAMAP-Rule MF_02121 Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. HAMAP-Rule MF_02121
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_02121
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis Methionine biosynthesis Threonine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' L-methionine biosynthetic process Inferred from electronic annotation. Source: HAMAP aspartate metabolic process Inferred from electronic annotation. Source: InterPro diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP isoleucine biosynthetic process Inferred from electronic annotation. Source: InterPro lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP threonine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: HAMAP aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 349

349

Aspartate-semialdehyde dehydrogenase HAMAP-Rule MF_02121

PRO_0000141380

Regions

Nucleotide binding

12 – 15

NADP By similarity

Nucleotide binding

39 – 40

NADP By similarity

Nucleotide binding

178 – 179

NADP By similarity

Nucleotide binding

326 – 327

NADP By similarity

Sites

Active site

148

Acyl-thioester intermediate By similarity

Active site

241

Proton acceptor By similarity

Binding site

113

Phosphate By similarity

Binding site

175

Substrate By similarity

Binding site

201

Substrate By similarity

Binding site

204

Phosphate By similarity

Binding site

234

Substrate By similarity

Experimental info

Sequence conflict

V → I in AAB21985. Ref.1

Sequence conflict

V → I in AAA25262. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P41394 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 1DB092D05CE66254
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FASTA

349

38,018

        10         20         30         40         50         60 
MSRVKVAVLG ATGSVGQRFI QLLDHHPFFE VTHLCASENS AGKTYGEVMK TRWKISSDIP 

        70         80         90        100        110        120 
AYAKNLVITT PDPAKTKDVV LAFSGLDSNV AGEVEKNYAN AGIHIISNSK NHRMDPTVPI 

       130        140        150        160        170        180 
LSAEVNSSHL EVLTSQKTKG KIITNSNCTI MGVTISLKPL LDRFGIESVM LFSMQAISGA 

       190        200        210        220        230        240 
GYPGVPTMDI LGNVIPHIGG EEEKAEIEPL KCLGKVENGK ILHADFSISA HCNRVPVFDG 

       250        260        270        280        290        300 
HTVCVSVKFK KKPSREEIIS SWKDFSGEPQ TLGLPLAPNP VILFREEEDR PQPRLDLDTG 

       310        320        330        340 
KGMTTVIGRL RPDPILDWKY VVLSHNTIRG AAGAALLNAE LLYKKKFLG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of dapD, aroD and asd of Leptospira interrogans serovar icterohaemorrhagiae, and nucleotide sequence of the asd gene." Baril C., Richaud C., Fourni E., Baranton G., Saint-Girons I. J. Gen. Microbiol. 138:47-53(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Serogroup Icterohaemorrhagiae.
[2]	"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing." Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. Zhao G.-P. Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 56601.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S92223 Genomic DNA. Translation: AAB21985.1. M77500 Genomic DNA. Translation: AAA25262.1. AE010301 Genomic DNA. Translation: AAN51914.1.
PIR	A44846.
RefSeq	NP_714899.1. NC_004343.2.
3D structure databases
ProteinModelPortal	P41394.
ModBase	Search...
Protein-protein interaction databases
STRING	189518.LB355.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN51914; AAN51914; LB_355.
GeneID	1153914.
KEGG	lil:LB_355.
PATRIC	22390238. VBILepInt91350_4670.
Phylogenomic databases
eggNOG	COG0136.
HOGENOM	HOG000013358.
KO	K00133.
OMA	VEEQFAK.
ProtClustDB	PRK08664.
Enzyme and pathway databases
BioCyc	LINT189518:GJBB-3740-MONOMER.
UniPathway	UPA00034; UER00016. UPA00050; UER00463. UPA00051; UER00464.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_02121. ASADH.
InterPro	IPR000319. Asp-semialdehyde_DH_CS. IPR005676. Asp_semi-ald_DH_pep-lack. IPR012080. Asp_semialdehyde_DH. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF000148. ASA_dh. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00978. asd_EA. 1 hit.
PROSITE	PS01103. ASD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHAS_LEPIN

Accession

Primary (citable) accession number: P41394

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 6, 2002
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents