A5PJR4 (PURA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Adenylosuccinate synthetase, basic isozyme
Adenylosuccinate synthetase, muscle isozyme
Short name=M-type adenylosuccinate synthetase
IMP--aspartate ligase 1

Gene names

Name:	ADSSL1
Synonyms:	ADSS1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP By similarity.
Catalytic activity	GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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
PTM	Phosphoprotein
Technical term	Complete proteome Reference 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 – 457	457	Adenylosuccinate synthetase isozyme 1		PRO_0000321960
Regions
	Nucleotide binding	42 – 48	7	GTP By similarity
	Nucleotide binding	70 – 72	3	GTP By similarity
	Nucleotide binding	363 – 365	3	GTP By similarity
	Nucleotide binding	445 – 448	4	GTP By similarity
	Region	43 – 46	4	IMP binding By similarity
	Region	68 – 71	4	IMP binding By similarity
	Region	331 – 337	7	Substrate binding By similarity
Sites
	Active site	43	1	Proton acceptor By similarity
	Active site	71	1	Proton donor By similarity
	Metal binding	43	1	Magnesium By similarity
	Metal binding	70	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	43	1	Substrate By similarity
	Binding site	163	1	IMP By similarity
	Binding site	177	1	IMP; shared with dimeric partner By similarity
	Binding site	256	1	IMP By similarity
	Binding site	271	1	IMP By similarity
	Binding site	335	1	IMP By similarity
	Binding site	337	1	GTP By similarity
Amino acid modifications
	Modified residue	388	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5PJR4 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: 202C6350F68068F5	FASTA	457	50,134
	10 20 30 40 50 60 MSGTRASNDR PPSAGGVKRG RLQHEAATTG SRVTVVLGAQ WGDEGKGKVV DLLATDADVV 70 80 90 100 110 120 SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NPKAVSFIGN GVVVHLPGLF EEAEKNEKKG 130 140 150 160 170 180 LKDWEKRLVI SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTRKGIGPA YSSKAARTGL 190 200 210 220 230 240 RICDLLSDFD EFSSRFKNLA RQHQSMFPSL EVDVEGQLKR LKGFAERIRP MVRDGVYFMY 250 260 270 280 290 300 EALHGPPKKI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGEVYGVVKA 310 320 330 340 350 360 YTTRVGIGAF PTEQINEIGD LLQSRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA 370 380 390 400 410 420 LTKLDILDAL DEIKVGVAYK LGGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE 430 440 450 DLPPQAQSYI RFVENHVGVA VKWVGVGKSR DSMIQLF

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal muscle.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC142211 mRNA. Translation: AAI42212.1.
IPI	IPI00707722.
RefSeq	NP_001092662.1. NM_001099192.1.
UniGene	Bt.16782.
3D structure databases
ProteinModelPortal	A5PJR4.
SMR	A5PJR4. Positions 29-457.
ModBase	Search...
Protein-protein interaction databases
STRING	A5PJR4.
Proteomic databases
PRIDE	A5PJR4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000044296; ENSBTAP00000041803; ENSBTAG00000017616.
GeneID	784089.
KEGG	bta:784089.
Organism-specific databases
CTD	122622.
Phylogenomic databases
eggNOG	maNOG07116.
GeneTree	ENSGT00390000015553.
HOVERGEN	HBG053768.
InParanoid	A5PJR4.
OrthoDB	EOG4P5K90.
Family and domain databases
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_BOVIN

Accession

Primary (citable) accession number: A5PJR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	July 10, 2007
Last modified:	November 16, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program