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A7ZML4 (ASTD_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:EcE24377A_1968
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length492 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

Inferred from electronic annotation. Source: InterPro

   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 – 492492N-succinylglutamate 5-semialdehyde dehydrogenase HAMAP MF_01174
PRO_1000065754

Regions

Nucleotide binding220 – 2256NAD By similarity

Sites

Active site2431 By similarity
Active site2771 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZML4 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: E0E721E467241BBD

FASTA49253,029
        10         20         30         40         50         60 
MTLWINGDWI TGQGASRVKR NPVSGEVLWQ GNDADAAQVG QACRAARAAF PRWARLSLAE 

        70         80         90        100        110        120 
RQVVVERFAG LLERNKGELT 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

References

[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].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV17826.1.
RefSeqYP_001463043.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZML4.
SMRA7ZML4. Positions 2-484.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZML4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000022567; EBESCP00000021629; EBESCG00000021621.
GeneID5586005.
GenomeReviewsGene locus EcE24377A_1968 in contig CP000800_GR.
KEGGecw:EcE24377A_1968.
PATRIC18293182. VBIEscCol31211_2244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
GeneTreeEBGT00050000009176.
HOGENOMHBG752218.
OMAKAYHART.
ProtClustDBPRK09457.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_1968-MONOMER.

Family and domain databases

HAMAPMF_01174. Aldedh_AstD.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR017649. SuccinylGlu_semiald_DH_AstD.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KOK06447.
PANTHERPTHR11699:SF24. PTHR11699:SF24. 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...

Entry information

Entry nameASTD_ECO24
AccessionPrimary (citable) accession number: A7ZML4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 35 of the entry and version 1 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