P30520 (PURA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Adenylosuccinate synthetase, acidic isozyme
Adenylosuccinate synthetase, liver isozyme
Short name=L-type adenylosuccinate synthetase
IMP--aspartate ligase 2

Gene names

Name:	ADSS
Synonyms:	ADSS2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. HAMAP-Rule MF_03127
Catalytic activity	GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP-Rule MF_03127
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP-Rule MF_03127
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm. Note: Partially associated with particulate fractions. HAMAP-Rule MF_03127
Sequence similarities	Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' AMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway AMP biosynthetic process Inferred from direct assay PubMed 2004783. Source: UniProtKB GTP catabolic process Inferred from electronic annotation. Source: Compara IMP metabolic process Inferred from electronic annotation. Source: Compara aspartate metabolic process Inferred from electronic annotation. Source: Compara cellular response to electrical stimulus Inferred from electronic annotation. Source: Compara immune system process Non-traceable author statement PubMed 15786719. Source: UniProtKB purine nucleobase metabolic process Traceable author statement. Source: Reactome response to ammonium ion Inferred from electronic annotation. Source: Compara response to purine-containing compound Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	GTP binding Non-traceable author statement PubMed 15786719Ref.1. Source: UniProtKB adenylosuccinate synthase activity Inferred from direct assay PubMed 2004783. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphate ion binding Non-traceable author statement PubMed 15786719Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 456

456

Adenylosuccinate synthetase isozyme 2 HAMAP-Rule MF_03127

PRO_0000095130

Regions

Nucleotide binding

39 – 45

7

GTP HAMAP-Rule MF_03127

Nucleotide binding

67 – 69

3

GTP HAMAP-Rule MF_03127

Nucleotide binding

362 – 364

3

GTP HAMAP-Rule MF_03127

Nucleotide binding

444 – 447

4

GTP HAMAP-Rule MF_03127

Region

40 – 43

4

IMP binding By similarity

Region

65 – 68

4

IMP binding By similarity

Region

330 – 336

7

Substrate binding By similarity

Sites

Active site

40

1

Proton acceptor By similarity

Active site

68

1

Proton donor By similarity

Metal binding

40

1

Magnesium By similarity

Metal binding

67

1

Magnesium; via carbonyl oxygen By similarity

Binding site

40

1

Substrate By similarity

Binding site

162

1

IMP By similarity

Binding site

176

1

IMP; shared with dimeric partner By similarity

Binding site

255

1

IMP By similarity

Binding site

270

1

IMP By similarity

Binding site

334

1

IMP By similarity

Binding site

336

1

GTP By similarity

Natural variations

Natural variant

179

1

L → F.
Corresponds to variant rs12134870 [ dbSNP | Ensembl ].

VAR_051881

Experimental info

Sequence conflict

24 – 25

2

RP → A in CAA47123. Ref.1

Secondary structure

1

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456

Helix Strand Turn

Details...

Beta strand

30 – 39

10

Helix

43 – 51

9

Beta strand

55 – 59

5

Beta strand

68 – 72

5

Beta strand

75 – 82

8

Helix

84 – 87

4

Beta strand

92 – 95

4

Beta strand

99 – 102

4

Helix

103 – 116

14

Helix

118 – 120

3

Helix

123 – 125

3

Beta strand

126 – 130

5

Beta strand

134 – 136

3

Helix

138 – 149

12

Helix

166 – 174

9

Helix

181 – 184

4

Helix

188 – 205

18

Helix

213 – 227

15

Helix

228 – 230

3

Helix

234 – 243

10

Beta strand

249 – 252

4

Helix

257 – 259

3

Turn

261 – 263

3

Helix

277 – 283

7

Helix

287 – 289

3

Beta strand

290 – 307

18

Helix

316 – 324

9

Turn

330 – 332

3

Beta strand

337 – 339

3

Helix

343 – 353

11

Beta strand

356 – 361

6

Helix

363 – 368

6

Beta strand

370 – 380

11

Beta strand

383 – 387

5

Helix

392 – 395

4

Beta strand

399 – 406

8

Helix

418 – 420

3

Helix

423 – 436

14

Beta strand

440 – 444

5

Beta strand

446 – 448

3

Beta strand

451 – 454

4

Sequences

	Sequence		Length	Mass (Da)
	P30520 [UniParc]. Last modified May 27, 2002. Version 3. Checksum: 23B7AAC58A238783	FASTA	456	50,097
	10 20 30 40 50 60 MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC 70 80 90 100 110 120 QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV IHLPGLFEEA EKNVQKGKGL 130 140 150 160 170 180 EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ RQEQAGKNLG TTKKGIGPVY SSKAARSGLR 190 200 210 220 230 240 MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE 250 260 270 280 290 300 ALHGPPKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 310 320 330 340 350 360 TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH MINGFTALAL 370 380 390 400 410 420 TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV QYKTLPGWNT DISNARAFKE 430 440 450 LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase." Powell S.M., Zalkin H., Dixon J.E. FEBS Lett. 303:4-10(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[2]	Stone R.L. Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Human adenylosuccinate synthetase isozyme 2 in complex with GDP." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-456 IN COMPLEX WITH GDP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X66503 Genomic DNA. Translation: CAA47123.1.
AL591594, AL645465 Genomic DNA. Translation: CAI14037.1.
AL645465, AL591594 Genomic DNA. Translation: CAI15031.1.
CH471148 Genomic DNA. Translation: EAW77102.1.
BC012356 mRNA. Translation: AAH12356.1.

IPI

IPI00026833.

PIR

S21166.

RefSeq

NP_001117.2. NM_001126.3.

UniGene

Hs.498313.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V40	X-ray	1.90	A	21-456	[»]

ProteinModelPortal

P30520.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30520. 4 interactions.

STRING

9606.ENSP00000355493.

PTM databases

PhosphoSite

P30520.

Polymorphism databases

DMDM

21264498.

Proteomic databases

PaxDb

P30520.

PeptideAtlas

P30520.

PRIDE

P30520.

Protocols and materials databases

DNASU

159.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366535; ENSP00000355493; ENSG00000035687.

GeneID

159.

KEGG

hsa:159.

UCSC

uc001iaj.3. human.

Organism-specific databases

CTD

159.

GeneCards

GC01M244571.

HGNC

HGNC:292. ADSS.

HPA

HPA024400.

MIM

103060. gene.

neXtProt

NX_P30520.

PharmGKB

PA24601.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0104.

HOGENOM

HOG000260959.

HOVERGEN

HBG053768.

InParanoid

P30520.

KO

K01939.

OMA

AMINGCT.

OrthoDB

EOG4P5K90.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00075; UER00335.

Gene expression databases

ArrayExpress

P30520.

Bgee

P30520.

CleanEx

HS_ADSS.

Genevestigator

P30520.

GermOnline

ENSG00000035687. Homo sapiens.

Family and domain databases

HAMAP

MF_03127. Adenylosucc_synth_vert_acid.

InterPro

IPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]

PANTHER

PTHR11846. PTHR11846. 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...

Other

BindingDB

P30520.

ChEMBL

CHEMBL4875.

DrugBank

DB00128. L-Aspartic Acid.

EvolutionaryTrace

P30520.

GenomeRNAi

159.

NextBio

633.

SOURCE

Search...

Entry information

Entry name

PURA2_HUMAN

Accession

Primary (citable) accession number: P30520
Secondary accession number(s): B1AQM5, Q96EG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	May 27, 2002
Last modified:	May 1, 2013
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.