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B9KJ18 (B9KJ18_ANAMF) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylosuccinate synthetase HAMAP MF_00011

Short name=AMPSase HAMAP MF_00011
Short name=AdSS HAMAP MF_00011
EC=6.3.4.4 HAMAP MF_00011
Alternative name(s):
IMP--aspartate ligase HAMAP MF_00011
Gene names
Name:purA HAMAP MF_00011
Ordered Locus Names:AMF_641
OrganismAnaplasma marginale (strain Florida) [Complete proteome] [HAMAP] EMBL ACM49480.1
Taxonomic identifier320483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP MF_00011

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding31 – 377GTP By similarity HAMAP MF_00011
Nucleotide binding59 – 613GTP By similarity HAMAP MF_00011
Nucleotide binding350 – 3523GTP By similarity HAMAP MF_00011
Nucleotide binding432 – 4343GTP By similarity HAMAP MF_00011
Region32 – 354IMP binding By similarity HAMAP MF_00011
Region57 – 604IMP binding By similarity HAMAP MF_00011
Region318 – 3247Substrate binding By similarity HAMAP MF_00011

Sites

Active site321Proton acceptor By similarity HAMAP MF_00011
Active site601Proton donor By similarity HAMAP MF_00011
Metal binding321Magnesium By similarity HAMAP MF_00011
Metal binding591Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011
Binding site1491IMP By similarity HAMAP MF_00011
Binding site1631IMP; shared with dimeric partner By similarity HAMAP MF_00011
Binding site2431IMP By similarity HAMAP MF_00011
Binding site2581IMP By similarity HAMAP MF_00011
Binding site3221IMP By similarity HAMAP MF_00011
Binding site3241GTP By similarity HAMAP MF_00011

Sequences

Sequence LengthMass (Da)Tools
B9KJ18 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 27748DBE496A4610

FASTA44548,533
        10         20         30         40         50         60 
MLTLFLYFAS LARNFHGHQM ASIVVVGLQW GDEGKGKIVD WLSVSADAVV RFQGGNNAGH 

        70         80         90        100        110        120 
TVVADGRVYK LSLLPTSVLR QNKLSMIGSG VALDPYALVR EVDSLKDSGI FLDPDSLCLS 

       130        140        150        160        170        180 
ESCPLVLSVH RDADSIMEEM RGNESIGTTC MGIGPCYEDK VGRRAIRLCD LLDETSLYDK 

       190        200        210        220        230        240 
VLCLLSYHNL LRRATNRREV TPHEIMDELT QIAPKVLPFM KPVPEIIVSL IKQGKTVLFE 

       250        260        270        280        290        300 
GAQGALLDID HGTYPYVTSS NTVAGYVRVG CGVGALGDMR VLGLAKAYTT RVGNGPFATE 

       310        320        330        340        350        360 
QTGTVGDAMF ERGREVGTVT NRVRRCGWFD AVSVRQAALS SGASEMVITK LDVLDTIDEI 

       370        380        390        400        410        420 
KVCTKYRCGE ESYDYLPAAS HIQNRLEPVY ETLPGWRTST LGAVSRSDLP ENAVSYISRL 

       430        440 
EELVGVPVSL VSTGPERNHI VPMNP 

« Hide

References

[1]"Conservation in the face of diversity: multistrain analysis of an intracellular bacterium."
Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E., Palmer G.H., Knowles D.P. Jr., Brayton K.A.
BMC Genomics 10:16-16(2009) [PubMed: 19134224] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001079 Genomic DNA. Translation: ACM49480.1.
RefSeqYP_002563736.1. NC_012026.1.

3D structure databases

ProteinModelPortalB9KJ18.
ModBaseSearch...

Protein-protein interaction databases

STRINGB9KJ18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7398077.
GenomeReviewsGene locus AMF_641 in contig CP001079_GR.
KEGGamf:AMF_641.
PATRIC20945206. VBIAnaMar82315_0735.

Organism-specific databases

CMRSearch...

Phylogenomic databases

ProtClustDBPRK01117.

Family and domain databases

HAMAPMF_00011. Adenylosucc_synth.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
KOK01939.
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
TIGRFAMsTIGR00184. PurA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB9KJ18_ANAMF
AccessionPrimary (citable) accession number: B9KJ18
Entry history
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)