Reviewed, UniProtKB/Swiss-Prot Q0AB55 (PURA_ALHEH)

Names and origin

Protein names

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

Gene names

Name:	purA
Ordered Locus Names:	Mlg_0578

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	432 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. 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
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 – 432	432	Adenylosuccinate synthetase HAMAP MF_00011		PRO_1000000772
Regions
	Nucleotide binding	13 – 19	7	GTP Potential
Sites
	Active site	141	1	By similarity
	Active site	148	1	By similarity
	Metal binding	14	1	Magnesium By similarity
	Metal binding	41	1	Magnesium; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0AB55-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: A71F370D4DA93DAE	FASTA	432	47,105
	10 20 30 40 50 60 MAKNVVVVGS QWGDEGKGKV VDLLTEHTGA VVRFQGGHNA GHTLVIDGEQ TILHLIPSGV 70 80 90 100 110 120 LREGVQCLIG NGVVLAPDAL LEEVQELEGK GVPARERLRI SPACPLILPC HVALDKAREA 130 140 150 160 170 180 ARGQARIGTT GRGIGPAYED KVSRRGIRVA DLFHRERLAA KLGELLDYHN FVLQHYFHEQ 190 200 210 220 230 240 PIDFQDVLER CLTYADELRP MVADIGQLLQ EHMDAGRDLL FEGAQGTLLD IDHGTYPFVT 250 260 270 280 290 300 SSNTVAGAAA TGTGIGPRDL HYVLGITKAY TTRVGSGPFP TELEDEIGDL LGERGREFGA 310 320 330 340 350 360 TTGRKRRCGW FDAVALRRAA QINSLSGLCI TKLDVLDELE TLRICIGYQC GDQLWESLPP 370 380 390 400 410 420 GAELLADCEP QYIDLPGWQS STLGVQQWDD LPENARAYLR KLEELIGVPV AIVSTGPDRK 430 ETIVLQNPFE SA

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI55932.1.
RefSeq	YP_741422.1.
3D structure databases
SMR	Q0AB55. Positions 4-431.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0AB55.
Genome annotation databases
GeneID	4268311.
GenomeReviews	Gene locus Mlg_0578 in contig CP000453_GR.
KEGG	aeh:Mlg_0578.
NMPDR	fig|187272.6.peg.551.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0104.
HOGENOM	HBG658237.
OMA	YVLGIIK.
PhylomeDB	Q0AB55.
Family and domain databases
HAMAP	MF_00011. Adenylosucc_synth. [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]
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_ALHEH

Accession

Primary (citable) accession number: Q0AB55

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 28 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)