O58187 (PURA_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
IMP--aspartate ligase

Gene names

Name:	purA
Ordered Locus Names:	PH0438

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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	3D-structure 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 – 339

339

Adenylosuccinate synthetase HAMAP MF_00011

PRO_0000095277

Regions

Nucleotide binding

12 – 18

7

GTP By similarity

Nucleotide binding

42 – 44

3

GTP By similarity

Nucleotide binding

284 – 286

3

GTP By similarity

Nucleotide binding

324 – 326

3

GTP By similarity

Region

13 – 16

4

IMP binding By similarity

Region

40 – 43

4

IMP binding By similarity

Region

252 – 258

7

Substrate binding By similarity

Sites

Active site

13

1

Proton acceptor By similarity

Active site

43

1

Proton donor By similarity

Metal binding

13

1

Magnesium By similarity

Metal binding

42

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

179

1

IMP By similarity

Binding site

194

1

IMP By similarity

Binding site

256

1

IMP By similarity

Binding site

258

1

GTP By similarity

Secondary structure

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339

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Helix

16 – 26

11

Beta strand

30 – 34

5

Beta strand

36 – 40

5

Beta strand

43 – 47

5

Beta strand

50 – 57

8

Turn

59 – 62

4

Beta strand

64 – 70

7

Helix

78 – 87

10

Helix

89 – 91

3

Helix

93 – 95

3

Beta strand

97 – 100

4

Helix

108 – 111

4

Helix

131 – 138

8

Turn

139 – 141

3

Helix

146 – 148

3

Beta strand

150 – 153

4

Helix

159 – 168

10

Beta strand

173 – 180

8

Helix

181 – 183

3

Turn

185 – 187

3

Helix

200 – 207

8

Helix

211 – 213

3

Beta strand

216 – 224

9

Beta strand

229 – 231

3

Helix

239 – 244

6

Turn

252 – 254

3

Beta strand

259 – 261

3

Helix

265 – 274

10

Beta strand

278 – 283

6

Helix

285 – 287

3

Helix

290 – 292

3

Helix

298 – 300

3

Helix

303 – 316

14

Beta strand

320 – 324

5

Beta strand

326 – 330

5

Beta strand

332 – 334

3

Sequences

	Sequence		Length	Mass (Da)
	O58187 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: ADA2FB1D07CCF3D0	FASTA	339	37,232
	10 20 30 40 50 60 MPSVIVVGGQ WGDEGKGSIV AYLSLHDEPE IIARGGVGTN AGHSVVINGK KYAVRQIPTG 70 80 90 100 110 120 FMQTKARLLI GAGVLVDPEV FFHELEQLKD FNVKDRVGID YRCAIIEEKH KQLDRTNGYL 130 140 150 160 170 180 HGKIGTTGSG CGPANADRVM RKAKQAKDVK ELEPYLTDVA QEINDALDEG SLVLVEGTQG 190 200 210 220 230 240 FGLSLYYGTY PYVTSKDVTA SSVAADVGIG PTRVDEVIVV FKSFPTRVGA GPFPTEMPME 250 260 270 280 290 300 EADRLGLVEY GTVTGRRRRV GWFDFEMARY SARINGATML AVTMLDKYDK EAFGVTDYDK 310 320 330 LPRKAKEFIE EIEERVGVPV GLIKTGPELE HIIDRRDTI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]	"Crystal structure of hypothetical adenylosuccinate synthetase, PH0438 from Pyrococcus horikoshii OT3." RIKEN structural genomics initiative (RSGI) Submitted (MAY-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA29524.1.

PIR

G71154.

RefSeq

NP_142419.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D7U	X-ray	2.50	A	1-339	[»]

ProteinModelPortal

O58187.

SMR

O58187. Positions 1-337.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001098; EBPYRP00000001098; EBPYRG00000001098.

GeneID

1444335.

GenomeReviews

Gene locus PH0438 in contig BA000001_GR.

KEGG

pho:PH0438.

NMPDR

fig|70601.1.peg.435.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000023069.

HOGENOM

HBG658237.

OMA

YVLGIIK.

ProtClustDB

PRK04293.

Enzyme and pathway databases

BioCyc

PHOR70601:PH0438-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]

PROSITE

PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PURA_PYRHO

Accession

Primary (citable) accession number: O58187

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program