Q3IIQ6 (PURA2_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate synthetase 2
Short name=AMPSase 2
Short name=AdSS 2
EC=6.3.4.4

Alternative name(s):
IMP--aspartate ligase 2

Gene names

Name:	purA2
Ordered Locus Names:	PSHAa1943

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	418 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 – 418	418	Adenylosuccinate synthetase 2 HAMAP MF_00011		PRO_0000224306
Regions
	Nucleotide binding	12 – 18	7	GTP By similarity
	Nucleotide binding	40 – 42	3	GTP By similarity
	Nucleotide binding	329 – 331	3	GTP By similarity
	Nucleotide binding	407 – 409	3	GTP By similarity
	Region	13 – 16	4	IMP binding By similarity
	Region	38 – 41	4	IMP binding By similarity
	Region	297 – 303	7	Substrate binding By similarity
Sites
	Active site	13	1	Proton acceptor By similarity
	Active site	41	1	Proton donor By similarity
	Metal binding	13	1	Magnesium By similarity
	Metal binding	40	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	127	1	IMP By similarity
	Binding site	141	1	IMP; shared with dimeric partner By similarity
	Binding site	239	1	IMP By similarity
	Binding site	301	1	IMP By similarity
	Binding site	303	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3IIQ6 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 2B1816C303E1FCE0	FASTA	418	45,407
	10 20 30 40 50 60 MPSIVVVGAN WGDEGKGRIV DFLAENASAS IRFQGGNNAG HTVVNDFGTF KLHQLPSGIF 70 80 90 100 110 120 NPDCIAVLGP GMVISPSALS EEIAEVKAAG VNVKLCISDR ATLCLPLHAL EDTLEELRLG 130 140 150 160 170 180 DAAYGSTRQG ISPAYGDRVM KKGILVGWLN QPDVLLERIQ FMLDWKMPQL KALYPSCDFS 190 200 210 220 230 240 QTAEEMTQWL LDVTAPWRAF ICNVTEPLKA LQKQNANLLF EAQLGAGRDL VYGEYPYTTS 250 260 270 280 290 300 SNVTAAYAGI GSGLPALRPE RVVAVAKSFS SSVGTGTLVT AMEEQDNFRE SANEYGAVTG 310 320 330 340 350 360 RPRDMGYFDA VATRNGVELQ AATEIALTKI DCLSGMKDLK ICVAYDGDHS ENPIWPQTAA 370 380 390 400 410 LSPVYENMQP WDEDITGCRT FDSLPIAAQQ YVERIEALMG VPITMVSVGP EREQMIIR

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: CAI87007.1.
RefSeq	YP_340450.1. NC_007481.1.
3D structure databases
ProteinModelPortal	Q3IIQ6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3IIQ6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3708143.
GenomeReviews	Gene locus PSHAa1943 in contig CR954246_GR.
KEGG	pha:PSHAa1943.
NMPDR	fig|326442.4.peg.2169.
PATRIC	32297483. VBIPseHal105694_1881.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0104.
HOGENOM	HBG658237.
OMA	MESWSED.
ProtClustDB	CLSK906169.
Enzyme and pathway databases
BioCyc	PHAL326442:PSHAA1943-MONOMER.
Family and domain databases
HAMAP	MF_00011. Adenylosucc_synth. Divergent sequence. [Tree]
InterPro	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]
PROSITE	PS01266. ADENYLOSUCCIN_SYN_1. False negative. PS00513. ADENYLOSUCCIN_SYN_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PURA2_PSEHT

Accession

Primary (citable) accession number: Q3IIQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program