Reviewed, UniProtKB/Swiss-Prot Q8TIM8 (PURA2_METAC)

Names and origin

Protein names

Recommended name:
    Adenylosuccinate synthetase 2
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase 2
    AdSS 2
    AMPSase 2

Gene names

Name:	purA2
Ordered Locus Names:	MA_4118

Organism

Methanosarcina acetivorans [Complete proteome] [HAMAP]

Taxonomic identifier

2214 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays an important role in the de novo pathway of purine nucleotide biosynthesis. 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.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011
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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: HAMAP adenylosuccinate synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 424	424	Adenylosuccinate synthetase 2 HAMAP MF_00011		PRO_0000095270
Regions
	Nucleotide binding	11 – 17	7	GTP Potential
Sites
	Active site	138	1	By similarity
	Metal binding	12	1	Magnesium By similarity
	Metal binding	39	1	Magnesium; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8TIM8-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: F285B7D8FD7ABB81	FASTA	424	46,759
	10 20 30 40 50 60 MFTIITGAQF GDEGKGKIVD LLAKDYDIVA RFQGGNNAGH TVRVGDEVYK LHLIPSGILL 70 80 90 100 110 120 DARVLIGPGV VLNPEVLAEE TAMFEKHGIK VDAEKLGVDA KTSIIMPYHI EMDGLREAAR 130 140 150 160 170 180 KTKIGTTKRG IGYAYIDKVA RDEIRMAELV DKERFLKRLE ELAPQKEKEI EAMGGDPKIV 190 200 210 220 230 240 RDPFLIQKYL ELGEQFASYV TDVSREINQA LDEGKHVMAE AAQGTHLDVI HGTQKFVTSS 250 260 270 280 290 300 STIAGSACAN LGVGPTRVGN VIAIVKAYIT RVGEGPLPTE LSGELGEKIQ KAGGEFGTTT 310 320 330 340 350 360 GRGRRCGWFD LPLLKKAIAL NGYTEISLTK LDVLTGLEPL RICVGYKYKG EDLDYPPELT 370 380 390 400 410 420 EDLWECSPVY EDLPGWETDL TEVKAYSELP ENAQNYIKRL EELMKVPINY ISVGPGREQT FKKE

References

[1]

"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B. Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE010299 Genomic DNA. Translation: AAM07466.1.
RefSeq	NP_618986.1.
3D structure databases
HSSP	HSSP built from PDB template 1ADE based on UniProtKB P12283.
ModBase	Search...
Genome annotation databases
GeneID	1476012.
GenomeReviews	Gene locus MA_4118 in contig AE010299_GR.
KEGG	mac:MA4118.
NMPDR	fig|188937.1.peg.4012.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8TIM8.
OMA	Q8TIM8. ERDDTIV.
Enzyme and pathway databases
BioCyc	MACE188937:MA4118-MON.
BRENDA	6.3.4.4. 275708.
Family and domain databases
HAMAP	MF_00011. [Tree]
InterPro	IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view]
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
ProDom	PD001188. Asucc_synthtase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00788. Adenylsucc_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR00184. purA. 1 hit.
PROSITE	PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PURA2_METAC

Accession

Primary (citable) accession number: Q8TIM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)