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Reviewed, UniProtKB/Swiss-Prot Q5WVZ4 (ASTD_LEGPL)

Last modified February 9, 2010. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    N-succinylglutamate 5-semialdehyde dehydrogenase
    EC=1.2.1.71
Alternative name(s):
    Succinylglutamic semialdehyde dehydrogenase
      Short name=SGSD
Gene names
Name: astD
Ordered Locus Names: lpl1666
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate By similarity. HAMAP MF_01174

Catalytic activity

N-succinyl-L-glutamate 5-semialdehyde + NAD+ + H2O = N-succinyl-L-glutamate + NADH. HAMAP MF_01174

Pathway

Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 4/5. HAMAP MF_01174

Sequence similarities

Belongs to the aldehyde dehydrogenase family. AstD subfamily.

Ontologies

Keywords
   Biological processArginine metabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine catabolic process to glutamate

Inferred from electronic annotation. Source: HAMAP

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionsuccinylglutamate-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495N-succinylglutamate 5-semialdehyde dehydrogenase HAMAP MF_01174
PRO_0000262405

Regions

Nucleotide binding228 – 2336NAD By similarity

Sites

Active site2511 By similarity
Active site2851 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WVZ4-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: DF2B04954B45501C

FASTA49554,521
        10         20         30         40         50         60 
MSKLQIIQSK GQYINGEWIK GNGLILESTN PASGTLLWQG NNATDEEIAN ACYVAHRALK 

        70         80         90        100        110        120 
SWANTSFEER ARYTKAFVEQ VEKNRDQLAR LISLETGKPL WESQTEVSSV IGKVNLSIQA 

       130        140        150        160        170        180 
YQERTWPKQT ETAEANACLR FKPHGVVVVL GAFNFPAHLS NGHIVPALLA GNTVLYKPSE 

       190        200        210        220        230        240 
HTPAVAELII QCWHDSGLPP GVINCLQGNA NCGNTLLSQD IQGVYFTGSY ATGLRIHQQF 

       250        260        270        280        290        300 
CNRPEIILAL EMGGNNPLVI DEVKDIDAAV YHTMLSTMIT AGQRCTCARR IIVPDSQTGD 

       310        320        330        340        350        360 
LFLERFAKAC KLMRIGSFDS QPEPFIGPVI SHVQALKHLH AQKQLVEMGG EIILPMSLLV 

       370        380        390        400        410        420 
EYTGLISPGI IDMTRAKNPP DEEIFAPFAQ IYRYNHFDEA IQLANQTRYG LSAGLLSDNK 

       430        440        450        460        470        480 
DHYLQFYQHI RAGLINWNRP TTGAASSLPF GGVGCSGNHR PSAYFAADYC AYPVASMEQP 

       490 
LLTTPAQRLP GLVLE 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH15906.1.
RefSeqYP_127005.1.

3D structure databases

SMRQ5WVZ4. Positions 10-439, 12-465.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WVZ4.

Genome annotation databases

GeneID3113691.
GenomeReviewsGene locus lpl1666 in contig CR628337_GR.
KEGGlpf:lpl1666.
NMPDRfig|297245.3.peg.1848.

Organism-specific databases

LegioListlpl1666.
CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHBG752218.
OMAKAYHART.
PhylomeDBQ5WVZ4.

Enzyme and pathway databases

BioCycLPNE297245:LPL1666-MONOMER.

Family and domain databases

HAMAPMF_01174. Aldedh_AstD.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR017649. SuccinylGlu_semiald_DH_AstD.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03240. arg_catab_astD. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASTD_LEGPL
AccessionPrimary (citable) accession number: Q5WVZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 23, 2004
Last modified: February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents