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Reviewed, UniProtKB/Swiss-Prot A8A0T8 (ASTD_ECOHS)

Last modified June 15, 2010. Version 21. 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
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Names and originHide

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:EcHS_A1829
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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Protein attributesHide

Sequence length492 AA.
Sequence statusComplete.
Protein existenceInferred from homology.
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General annotation (Comments)Hide

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.

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OntologiesHide

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...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492N-succinylglutamate 5-semialdehyde dehydrogenase HAMAP MF_01174
PRO_1000065755

Regions

Nucleotide binding220 – 2256NAD By similarity

Sites

Active site2431 By similarity
Active site2771 By similarity
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SequencesHide

Sequence LengthMass (Da)Tools
A8A0T8-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 64AEF9CAC0E7DA5F

FASTA49252,988
        10         20         30         40         50         60 
MTLWINGDWI TGQGASRVKR NPVSGEVLWQ GNDAGAAQVE QACRAARAAF PRWARLSLAE 

        70         80         90        100        110        120 
RQVVVERFAG LLESNKAELT AIIARETGKP RWEAATEVTA MINKIAISIK AYHVRTGEQR 

       130        140        150        160        170        180 
SEMPDGAASL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTIIFKPS ELTPWSGEAV 

       190        200        210        220        230        240 
MRLWQQAGLP PGVLNLVQGG RETGQALSAL EDLDGLLFTG SANTGYQLHR QLSGQPEKIL 

       250        260        270        280        290        300 
ALEMGGNNPL IIDEVADIDA AVHLTIQSAF VTAGQRCTCA RRLLLKSGAQ GDAFLARLVA 

       310        320        330        340        350        360 
VSQRLTPGNW DDEPQPFIGG LISEQAAQQV VTAWQQLEAM GGRTLLAPRL LQSETSLLTP 

       370        380        390        400        410        420 
GIIEMTGVAG VPDEEVFGPL LRVWRYDSFE EAILMANNTR FGLSCGLVSP EREKFDQLLL 

       430        440        450        460        470        480 
EARAGIVNWN KPLTGAASTA PFGGIGASGN HRPSAWYAAD YCAWPMASLE SDSLTLPATL 

       490 
NPGLDFSDEV VR 

« Hide

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ReferencesHide

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV06142.1.
RefSeqYP_001458525.1.

3D structure databases

SMRA8A0T8. Positions 3-462.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8A0T8.

Genome annotation databases

EnsemblBacteriaEBESCT00000054896; EBESCP00000052881; EBESCG00000053944.
GeneID5591866.
GenomeReviewsGene locus EcHS_A1829 in contig CP000802_GR.
KEGGecx:EcHS_A1829.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHBG752218.
OMAKAYHART.
ProtClustDBPRK09457.

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]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR03240. arg_catab_astD. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...
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Entry informationHide

Entry nameASTD_ECOHS
AccessionPrimary (citable) accession number: A8A0T8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: June 15, 2010
This is version 21 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)
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Relevant documentsHide

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