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P30903 (DHAS_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:NMB2079
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Protein existenceInferred 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 MF_02121

Catalytic activity

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. HAMAP MF_02121

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. HAMAP MF_02121

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. HAMAP MF_02121

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. HAMAP MF_02121

Subunit structure

Homodimer.

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371Aspartate-semialdehyde dehydrogenase HAMAP MF_02121
PRO_0000141385

Regions

Nucleotide binding9 – 124NADP By similarity
Nucleotide binding37 – 382NADP By similarity
Nucleotide binding165 – 1662NADP By similarity

Sites

Active site1351Acyl-thioester intermediate By similarity
Active site2751Proton acceptor By similarity
Binding site731NADP By similarity
Binding site1021Phosphate By similarity
Binding site1621Substrate By similarity
Binding site1931NADP; via carbonyl oxygen By similarity
Binding site2411Substrate By similarity
Binding site2441Phosphate By similarity
Binding site2681Substrate By similarity
Binding site3511NADP By similarity

Experimental info

Sequence conflict441A → R in CAA78444. Ref.2
Sequence conflict117 – 1193DVL → NVI in CAA78444. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P30903 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: F36BF70BB80075AA

FASTA37139,858
        10         20         30         40         50         60 
MKVGFVGWRG MVGSVLMQRM KEENDFAHIP EAFFFTTSNV GGAAPDFGQA AKTLLDANNV 

        70         80         90        100        110        120 
AELAKMDIIV TCQGGDYTKS VFQALRDSGW NGYWIDAASS LRMKDDAIIV LDPVNRDVLD 

       130        140        150        160        170        180 
NGLKNGVKNY IGGNCTVSLM LMALGGLFQN DLVEWATSMT YQAASGAGAK NMRELISGMG 

       190        200        210        220        230        240 
AVHAQVADAL ADPAGSILDI DRKVSDFLRS EDYPKANFGV PLAGSLIPWI DVDLGNGQSK 

       250        260        270        280        290        300 
EEWKGGVETN KILGRSDNPT VIDGLCVRVG AMRCHSQAIT LKLKKDLPVS EIETILAGAN 

       310        320        330        340        350        360 
DWVKVIPNEK EASIHELTPA KVTGTLSVPV GRIRKLGMGG EYISAFTVGD QLLWGAAEPL 

       370 
RRVLRIVLGS L

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002098 Genomic DNA. Translation: AAF42397.1.
Z14063 Genomic DNA. Translation: CAA78444.1.
PIRE81009.
RefSeqNP_275068.1. NC_003112.2.

3D structure databases

ProteinModelPortalP30903.
SMRP30903. Positions 1-369.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000009379; EBNEIP00000008999; EBNEIG00000009379.
GeneID903977.
GenomeReviewsGene locus NMB2079 in contig AE002098_GR.
KEGGnme:NMB2079.
NMPDRfig|122586.1.peg.2002.
PATRIC20360326. VBINeiMen85645_2660.
TIGRNMB2079.

Phylogenomic databases

GeneTreeEBGT00050000020336.
HOGENOMHBG289760.
OMAIDGLCVR.
ProtClustDBPRK06598.

Enzyme and pathway databases

BioCycNMEN122586:NMB_2079-MONOMER.

Family and domain databases

HAMAPMF_02121. ASADH.
[Tree]
InterProIPR000319. Asp-semialdehyde_DH_CS.
IPR011534. Asp_ADH_gamma-type.
IPR012080. Asp_semialdehyde_DH.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00133.
PfamPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFPIRSF000148. ASA_dh. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01745. Asd_gamma. 1 hit.
PROSITEPS01103. ASD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHAS_NEIMB
AccessionPrimary (citable) accession number: P30903
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 1, 2000
Last modified: January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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