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P0C115

- PURA_BRUAB

UniProt

P0C115 - PURA_BRUAB

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Protein

Adenylosuccinate synthetase

Gene

purA

Organism
Brucella abortus biovar 1 (strain 9-941)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP By similarity.By similarity

Catalytic activityi

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131Proton acceptorUniRule annotation
Metal bindingi13 – 131MagnesiumUniRule annotation
Metal bindingi40 – 401Magnesium; via carbonyl oxygenUniRule annotation
Active sitei41 – 411Proton donorUniRule annotation
Binding sitei129 – 1291IMPUniRule annotation
Binding sitei143 – 1431IMP; shared with dimeric partnerUniRule annotation
Binding sitei223 – 2231IMPUniRule annotation
Binding sitei238 – 2381IMPUniRule annotation
Binding sitei302 – 3021IMPUniRule annotation
Binding sitei304 – 3041GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 187GTPUniRule annotation
Nucleotide bindingi40 – 423GTPUniRule annotation
Nucleotide bindingi330 – 3323GTPUniRule annotation
Nucleotide bindingi412 – 4143GTPUniRule annotation

GO - Molecular functioni

  1. adenylosuccinate synthase activity Source: UniProtKB-HAMAP
  2. GTP binding Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBABO262698:GJC2-1708-MONOMER.
UniPathwayiUPA00075; UER00335.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetaseUniRule annotation (EC:6.3.4.4UniRule annotation)
Short name:
AMPSaseUniRule annotation
Short name:
AdSSUniRule annotation
Alternative name(s):
IMP--aspartate ligaseUniRule annotation
Gene namesi
Name:purAUniRule annotation
Ordered Locus Names:BruAb1_1668
OrganismiBrucella abortus biovar 1 (strain 9-941)
Taxonomic identifieri262698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000540: Chromosome I

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Adenylosuccinate synthetasePRO_0000095153Add
BLAST

Proteomic databases

PRIDEiP0C115.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi262698.BruAb1_1668.

Structurei

3D structure databases

ProteinModelPortaliP0C115.
SMRiP0C115. Positions 2-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 164IMP bindingUniRule annotation
Regioni38 – 414IMP bindingUniRule annotation
Regioni298 – 3047Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0104.
HOGENOMiHOG000260959.
KOiK01939.
OMAiITTGAER.
OrthoDBiEOG68Q0QG.

Family and domain databases

HAMAPiMF_00011. Adenylosucc_synth.
InterProiIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11846. PTHR11846. 1 hit.
PfamiPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTiSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00184. purA. 1 hit.
PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C115-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MANVVVVGSQ WGDEGKGKIV DWLSERADVI VRYQGGHNAG HTLVIDGVSY
60 70 80 90 100
KLSLLPSGLV RGKLSVIGNG VVVDPHHFVA EVEKLRGQGI DVTPDVLRVA
110 120 130 140 150
ENAPLILSIH RELDAMREGS NSGLKIGTTK RGIGPAYEDK VGRRAIRVID
160 170 180 190 200
LTEPETLRPK VERLLAHHNS LRRGMGLEEI AVETILTELT SVADQILPYI
210 220 230 240 250
DQVWRVLDER RKAGARILFE GAQGALLDND HGTYPFVTSS NTVAGQAAAG
260 270 280 290 300
SGLGPTAIGY VLGITKAYTT RVGEGPFPTE LNDEIGEFLG TKGHEFGVVT
310 320 330 340 350
GRKRRCGWFD AVIVRQTVRT SGINGIALTK LDVLDGLEEI KICVAYELDG
360 370 380 390 400
KRIDYLPSSM GAQARVKPIY ETLPGWSETT AGARSWNDLP AQAVKYVRHI
410 420
EELIGAPVAM LSTSPEREDT ILVTDPFHD
Length:429
Mass (Da):46,561
Last modified:February 7, 2006 - v1
Checksum:iDF90E83E30690FF2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017223 Genomic DNA. Translation: AAX74987.1.
RefSeqiYP_222348.1. NC_006932.1.

Genome annotation databases

EnsemblBacteriaiAAX74987; AAX74987; BruAb1_1668.
GeneIDi3340306.
KEGGibmb:BruAb1_1668.
PATRICi17825118. VBIBruAbo15061_1761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017223 Genomic DNA. Translation: AAX74987.1 .
RefSeqi YP_222348.1. NC_006932.1.

3D structure databases

ProteinModelPortali P0C115.
SMRi P0C115. Positions 2-428.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262698.BruAb1_1668.

Proteomic databases

PRIDEi P0C115.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAX74987 ; AAX74987 ; BruAb1_1668 .
GeneIDi 3340306.
KEGGi bmb:BruAb1_1668.
PATRICi 17825118. VBIBruAbo15061_1761.

Phylogenomic databases

eggNOGi COG0104.
HOGENOMi HOG000260959.
KOi K01939.
OMAi ITTGAER.
OrthoDBi EOG68Q0QG.

Enzyme and pathway databases

UniPathwayi UPA00075 ; UER00335 .
BioCyci BABO262698:GJC2-1708-MONOMER.

Family and domain databases

HAMAPi MF_00011. Adenylosucc_synth.
InterProi IPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11846. PTHR11846. 1 hit.
Pfami PF00709. Adenylsucc_synt. 1 hit.
[Graphical view ]
SMARTi SM00788. Adenylsucc_synt. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00184. purA. 1 hit.
PROSITEi PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
    Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
    J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 9-941.

Entry informationi

Entry nameiPURA_BRUAB
AccessioniPrimary (citable) accession number: P0C115
Secondary accession number(s): P52004, Q57BJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: October 29, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella abortus strain 9-941
    Brucella abortus (strain 9-941): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3