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Reviewed, UniProtKB/Swiss-Prot Q5QVX3 (ASTD_IDILO)

Last modified November 25, 2008. Version 31. 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: IL2316
OrganismIdiomarina loihiensis [Complete proteome] [HAMAP]
Taxonomic identifier135577 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length489 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(+) + H(2)O = N-succinyl-L-glutamate + NADH.

Pathway

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

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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489N-succinylglutamate 5-semialdehyde dehydrogenase
PRO_0000262404

Regions

Nucleotide binding223 – 2286NAD By similarity

Sites

Active site2461 By similarity
Active site2801 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QVX3-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: A431DCD1D149BDFF

FASTA48953,046
        10         20         30         40         50         60 
MTNSIQFIDG CWEAGEGQLF KSIDPARNEV IWSGEAASET QVEKAILAAR AAFPDWSGRS 

        70         80         90        100        110        120 
VEERLAICQK FSELLEENKE HLARTMAKET GKPVWETRTE VGAMMGKVAI SERAYHERTG 

       130        140        150        160        170        180 
TVENDMPGAK AFIRHKPHGV VAVYGPYNFP GHLPNGHIVP ALIAGNTVVF KPSELTPMVA 

       190        200        210        220        230        240 
QETVKLWEKA GIPAGVLNLV QGEVDTGKAL SAHPQIDGLY FTGSSNTGHL LHKQFGGRPD 

       250        260        270        280        290        300 
KILALEMGGN NPLLVTNVAD VDAAVHNIVQ SAFITSGQRC TCARRLFIED SEQGRAVLER 

       310        320        330        340        350        360 
LIEVTENILV DDYEADPQPF MGAMISAKAA GEMVDAQNEL LHKGAKSLVR MKQTDSKKGF 

       370        380        390        400        410        420 
VTPGIVDVTG VEDLPDEEHF GPLLKVYRFK DIDAAIKEAN NTRYGLSAGV LCDDEQTYRY 

       430        440        450        460        470        480 
FFKHIRAGIV NWNKPITGAS SAAPFGGIGA SGNHRASAYY AADYCAYPVA SVEADSMSLP 


ESLAPGLKF 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L2-TR / ATCC BAA-735 / DSM 15497.

Cross-references

Sequence databases

AE017340 Genomic DNA. Translation: AAV83148.1.
RefSeqYP_156697.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3174410.
GenomeReviewsGene locus IL2316 in contig AE017340_GR.
KEGGilo:IL2316.
NMPDRfig|283942.3.peg.2303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5QVX3.

Enzyme and pathway databases

BioCycILOI283942:IL2316-MON.

Family and domain databases

HAMAPMF_01174.
[Tree]
InterProIPR016160. Ald_DHase_CS.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
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]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASTD_IDILO
AccessionPrimary (citable) accession number: Q5QVX3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: January 4, 2005
Last modified: November 25, 2008
This is version 31 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