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Reviewed, UniProtKB/Swiss-Prot A1U5W8 (ASTD_MARAV)

Last modified November 3, 2009. Version 29. 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: Maqu_3316
OrganismMarinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845)) [Complete proteome] [HAMAP]
Taxonomic identifier351348 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeMarinobacter

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

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 – 491491N-succinylglutamate 5-semialdehyde dehydrogenase HAMAP MF_01174
PRO_1000138051

Regions

Nucleotide binding225 – 2306NAD By similarity

Sites

Active site2481 By similarity
Active site2821 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1U5W8-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 52F36E678DD2AED1

FASTA49152,483
        10         20         30         40         50         60 
MANLTGNVYI DGLWLPGHGA PFESVQPVTG ETVWDGNAAS LEDVDAAVRE ARKAFLAWRR 

        70         80         90        100        110        120 
KSLAERQAVI EAFGELLEAN KEELAHQIGL ETGKPLWESR TEVAAMMGKI PISVKAYNER 

       130        140        150        160        170        180 
TGHTESDVAG GHAVLRHRPH GVVAVFGPYN FPGHLPNGHI VPALLAGNTV VFKPSELTPG 

       190        200        210        220        230        240 
VAELTVRLWE KAGLPDGVIN LVQGGSDTGK CLARHSLIDG LFFTGSSTVG HLLHEQFGGQ 

       250        260        270        280        290        300 
PEKILALEMG GNNPLIVQNV SDLDGAVHHA LQSAFLSAGQ RCTCARRLLV PKGKKGDEFL 

       310        320        330        340        350        360 
ARLVEVAARI TVAEFDADPQ PFMGSVISAE AANQLLKAQA AMLEKGATSL LEMKQLKPDT 

       370        380        390        400        410        420 
GLLSPGIVDA TGIELEDQEF FGPLLTVYRY KGFDEALELA NNTRYGLSAG ILSDDRKLYN 

       430        440        450        460        470        480 
RLVEEVRAGI VNWNRPLTGA SSAAPFGGVG ASGNHRPSAY YAADYCAWPM ASLEAGKSEL 

       490 
PDSLAPGLNF D 

« Hide

References

[1]"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000514 Genomic DNA. Translation: ABM20387.1.
RefSeqYP_960574.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1U5W8.

Genome annotation databases

GeneID4653619.
GenomeReviewsGene locus Maqu_3316 in contig CP000514_GR.
KEGGmaq:Maqu_3316.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIRAHDER.

Family and domain databases

HAMAPMF_01174.
[Tree]
InterProIPR016160. 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. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASTD_MARAV
AccessionPrimary (citable) accession number: A1U5W8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 29 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