Q1IJT2 (PURA_KORVE) 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:	Acid345_3868

Organism

Koribacter versatilis (strain Ellin345)

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	442 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 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 – 442	442	Adenylosuccinate synthetase HAMAP MF_00011		PRO_0000321789
Regions
	Nucleotide binding	16 – 22	7	GTP By similarity
	Nucleotide binding	44 – 46	3	GTP By similarity
	Nucleotide binding	335 – 337	3	GTP By similarity
	Nucleotide binding	417 – 419	3	GTP By similarity
	Region	17 – 20	4	IMP binding By similarity
	Region	42 – 45	4	IMP binding By similarity
	Region	303 – 309	7	Substrate binding By similarity
Sites
	Active site	17	1	Proton acceptor By similarity
	Active site	45	1	Proton donor By similarity
	Metal binding	17	1	Magnesium By similarity
	Metal binding	44	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	133	1	IMP By similarity
	Binding site	147	1	IMP; shared with dimeric partner By similarity
	Binding site	228	1	IMP By similarity
	Binding site	243	1	IMP By similarity
	Binding site	307	1	IMP By similarity
	Binding site	309	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1IJT2 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 565713090CC655DB	FASTA	442	47,644
	10 20 30 40 50 60 MVSKGKTAVV IGAQWGDEGK GKIVDVLSEN FRVVARYAGG HNAGHTVLIG GKKFVLQLIP 70 80 90 100 110 120 CGVLRPGCRG VIGNGVVLDP IAFLNEVQRL RDLGVAVDGN LFVSSRAHVI LPYHRMVELA 130 140 150 160 170 180 SENAPGRVKI GTTSRGIGPS YEDKMGRRGL RVADLLDSTL LKKHIENACK EKNTIVHALF 190 200 210 220 230 240 NAEPIDPDKM YNEYAKAAEK VAPFVTDTAV LLNNAINSGE SVMFEGAQGT MLDIDHGTYP 250 260 270 280 290 300 FVTSSSATSG GAVIGTGVPP TSISTVIGVT KAYCTRVGEG PFPSELHDAM GDAIRKKGNE 310 320 330 340 350 360 FGAVTGRPRR TGWLDLPLLR YSNMINGTEW LVVTKLDVLD ELDEIPVATS YKIDGKESEE 370 380 390 400 410 420 IPAQGCGFDK IEPIYTKLPG WKTDTTKISK YEDLPAKTKE YLKFVEQQSG AKVGILSTGP 430 440 DRDQSIYTDA FVNALGLKHL GK

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin345.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000360 Genomic DNA. Translation: ABF42868.1.
RefSeq	YP_592942.1. NC_008009.1.
3D structure databases
ProteinModelPortal	Q1IJT2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IJT2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4071020.
GenomeReviews	Gene locus Acid345_3868 in contig CP000360_GR.
KEGG	aba:Acid345_3868.
NMPDR	fig|204669.6.peg.3855.
PATRIC	31984992. VBICanKor57425_4124.
Phylogenomic databases
eggNOG	COG0104.
HOGENOM	HBG658237.
OMA	SRCQGGN.
PhylomeDB	Q1IJT2.
ProtClustDB	PRK01117.
Enzyme and pathway databases
BioCyc	ABAC204669:ACID345_3868-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]
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

PURA_KORVE

Accession

Primary (citable) accession number: Q1IJT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program