Q3IEZ3 (PURA1_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate synthetase 1
Short name=AMPSase 1
Short name=AdSS 1
EC=6.3.4.4

Alternative name(s):
IMP--aspartate ligase 1

Gene names

Name:	purA1
Ordered Locus Names:	PSHAa0275

Organism

Pseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]

Taxonomic identifier

326442 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP By similarity. HAMAP MF_00011
Catalytic activity	GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP MF_00011
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00011
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011
Subunit structure	Homodimer By similarity. HAMAP MF_00011
Subcellular location	Cytoplasm By similarity HAMAP MF_00011.
Sequence similarities	Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylosuccinate synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding 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 – 437	437	Adenylosuccinate synthetase 1 HAMAP MF_00011		PRO_0000224305
Regions
	Nucleotide binding	13 – 19	7	GTP By similarity
	Nucleotide binding	41 – 43	3	GTP By similarity
	Nucleotide binding	338 – 340	3	GTP By similarity
	Nucleotide binding	421 – 423	3	GTP By similarity
	Region	14 – 17	4	IMP binding By similarity
	Region	39 – 42	4	IMP binding By similarity
	Region	306 – 312	7	Substrate binding By similarity
Sites
	Active site	14	1	Proton acceptor By similarity
	Active site	42	1	Proton donor By similarity
	Metal binding	14	1	Magnesium By similarity
	Metal binding	41	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	130	1	IMP By similarity
	Binding site	144	1	IMP; shared with dimeric partner By similarity
	Binding site	225	1	IMP By similarity
	Binding site	240	1	IMP By similarity
	Binding site	310	1	IMP By similarity
	Binding site	312	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3IEZ3 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 70B76AC4238B6964	FASTA	437	47,120
	10 20 30 40 50 60 MGKNVVVLGT QWGDEGKGKV VDLLTDKASL VVRYQGGHNA GHTLVIDGEK TVLHLIPSGV 70 80 90 100 110 120 LRDNVKCVIG NGVVLSPEAL MREIGMLEAR GVPVRERLLI SAACPLILPF HVALDVARET 130 140 150 160 170 180 ARGDKPIGTT GRGIGPAYED KVARRGLRVG DLFNPELFAA KLEEVLEYHN FTLVNYYKVD 190 200 210 220 230 240 AVDFQKTFDD AMAVADILKA MIVDVTELLD QTRLAGDNIL FEGAQGTLLD IDHGTYPYVT 250 260 270 280 290 300 SSNTTAGGVA TGAGFGPLHL DYVLGIIKAY TTRVGSGPFP TELYDGLDKQ DPVGKHLGDK 310 320 330 340 350 360 GHEFGATTGR LRRTGWLDAV AMRRAVQINS ISGFCLTKLD VLDGLETLKI CTGYKLEDGT 370 380 390 400 410 420 VTNVTPLAAE GYEKVTPIYE EMPGWSENTV GVTSLDGLPK AAIDYVKRIE ELTGVPVDII 430 STGPDRVETM ILRNPFA

References

[1]

"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125." Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A. Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TAC 125.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR954246 Genomic DNA. Translation: CAI85374.1.
RefSeq	YP_338817.1. NC_007481.1.
3D structure databases
ProteinModelPortal	Q3IEZ3.
SMR	Q3IEZ3. Positions 2-436.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3IEZ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3709931.
GenomeReviews	Gene locus PSHAa0275 in contig CR954246_GR.
KEGG	pha:PSHAa0275.
NMPDR	fig|326442.4.peg.111.
PATRIC	32294085. VBIPseHal105694_0262.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0104.
HOGENOM	HBG658237.
OMA	YVLGIIK.
PhylomeDB	Q3IEZ3.
ProtClustDB	PRK01117.
Enzyme and pathway databases
BioCyc	PHAL326442:PSHAA0275-MONOMER.
Family and domain databases
HAMAP	MF_00011. Adenylosucc_synth. [Tree]
InterPro	IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view]
KO	K01939.
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
SMART	SM00788. Adenylsucc_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR00184. PurA. 1 hit.
PROSITE	PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PURA1_PSEHT

Accession

Primary (citable) accession number: Q3IEZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program