Q63SD7 (ASTD_BURPS) Reviewed, UniProtKB/Swiss-Prot

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:	BPSL2387

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Arginine metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	succinylglutamate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 487	487	N-succinylglutamate 5-semialdehyde dehydrogenase HAMAP MF_01174		PRO_0000262389
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)
	Q63SD7 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: DB57627D1A743BA2	FASTA	487	51,839
	10 20 30 40 50 60 MTELFIDGAW RDGAGPVFAS RNPGTGEPVW EGAGASADDV ERAVASARRA FAAWSALDLD 70 80 90 100 110 120 ARCAIVKRFA ALLVERKEAL ATMIGRETGK PLWEARTEVA SMAAKVDVSI AAYHERTGER 130 140 150 160 170 180 RSPTADGVAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVVFKP SELAPGVARA 190 200 210 220 230 240 TVEIWRDAGL PAGVLNLVQG EKDTGVALAN HRQIDGLFFT GSSDTGTLLH RQFGGRPEIV 250 260 270 280 290 300 LALEMGGNNP LVVADVEDID AAVHHAIQSA FLSAGQRCTC ARRILVPRGA FGDRFLERFA 310 320 330 340 350 360 DVASRITADV YDADPQPFMG AVISARAASR LVAAQAKLLE LGAAPIIEMR QRDPALGFVN 370 380 390 400 410 420 ASILDVTPVR ELPDEEHFGP LAQIVRYTDL DDAIARANDT AFGLSAGLLA DDETVWNTFR 430 440 450 460 470 480 RAIRAGIVNW NRPTNGASSA APFGGAGRSG NHRPSAYYAA DYCAYPMASV ESAQLQMPAN LSPGLHF

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH36389.1.
RefSeq	YP_108979.1. NC_006350.1.
3D structure databases
ProteinModelPortal	Q63SD7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3093486.
GenomeReviews	Gene locus BPSL2387 in contig BX571965_GR.
KEGG	bps:BPSL2387.
PATRIC	19265025. VBIBurPse99623_2720.
Phylogenomic databases
HOGENOM	HBG752218.
OMA	MTQRDPR.
PhylomeDB	Q63SD7.
ProtClustDB	PRK09457.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL2387-MONOMER.
Family and domain databases
HAMAP	MF_01174. Aldedh_AstD. [Tree]
InterPro	IPR016161. 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]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KO	K06447.
PANTHER	PTHR11699:SF24. PTHR11699:SF24. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR03240. Arg_catab_astD. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASTD_BURPS

Accession

Primary (citable) accession number: Q63SD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program