Reviewed, UniProtKB/Swiss-Prot Q7NXX7 (ASTD_CHRVO)

Names and origin

Protein names

Recommended 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:	CV_1499

Organism

Chromobacterium violaceum [Complete proteome] [HAMAP]

Taxonomic identifier

536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Arginine metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process to glutamate Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	succinylglutamate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 486	486	N-succinylglutamate 5-semialdehyde dehydrogenase		PRO_0000262396
Regions
	Nucleotide binding	221 – 226	6	NAD By similarity
Sites
	Active site	244	1	By similarity
	Active site	278	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7NXX7-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: AF4A8914405CE27A	FASTA	486	51,073
	10 20 30 40 50 60 MSSLFIDGKW LAGDGEAMAK TNPADNAPLW QGRAASAAQV DAAVRAARAA FPAWARMGLE 70 80 90 100 110 120 ERAKVVRRFG ERLTERKAEL ARVIAQETGK PLWEATTEVT TMVGKIDISL KALAERTGER 130 140 150 160 170 180 AAAMGDAQAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNSVIFKP SELTPWTAEE 190 200 210 220 230 240 TVKLWAEAGL PAGVIGLVQG AKDTGVALAG HEGLDGLFFT GSSATGALLH KQFSGRPDKI 250 260 270 280 290 300 LALEMGGNNP LIVGEVADVD GAVHHVIQSA FVSAGQRCTC ARRLLVPQGE WGDAFVARLV 310 320 330 340 350 360 EVAGKLRVGK FDAEPAPFLG AVISNAAADA LLKAQDDLVA AGGTPLLAMR RLEEGAAMLT 370 380 390 400 410 420 PGIIDTTAAV RPDEEFFGPL LQVIRYADFD QAIAIANDTR FGLAGGVLSD SRELYDRYWL 430 440 450 460 470 480 ESRAGVVNWN KPLTGASSAA PFGGIGASGN HRPSAYYAAD YCAYPVASLE CDSLALPAQL SPGIVL

References

[1]

"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G. Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016825 Genomic DNA. Translation: AAQ59174.1.
RefSeq	NP_901169.1.
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBase	Search...
Genome annotation databases
GeneID	2549965.
GenomeReviews	Gene locus CV_1499 in contig AE016825_GR.
KEGG	cvi:CV_1499.
NMPDR	fig|243365.1.peg.1499.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7NXX7.
Enzyme and pathway databases
BioCyc	CVIO243365:CV_1499-MON.
Family and domain databases
HAMAP	MF_01174. [Tree]
InterPro	IPR016160. Ald_DHase_CS. IPR016162. Ald_DHase_N. IPR015590. Aldehyde_DHase. IPR017649. SuccinylGlu_semiald_DH_AstD. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASTD_CHRVO

Accession

Primary (citable) accession number: Q7NXX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	December 15, 2003
Last modified:	November 25, 2008
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)