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A1TM37 (PURA_ACIAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:Aave_1434
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length459 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.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Adenylosuccinate synthetase HAMAP MF_00011
PRO_0000321790

Regions

Nucleotide binding18 – 247GTP By similarity
Nucleotide binding46 – 483GTP By similarity
Nucleotide binding359 – 3613GTP By similarity
Nucleotide binding441 – 4433GTP By similarity
Region19 – 224IMP binding By similarity
Region44 – 474IMP binding By similarity
Region327 – 3337Substrate binding By similarity

Sites

Active site191Proton acceptor By similarity
Active site471Proton donor By similarity
Metal binding191Magnesium By similarity
Metal binding461Magnesium; via carbonyl oxygen By similarity
Binding site1381IMP By similarity
Binding site1521IMP; shared with dimeric partner By similarity
Binding site2481IMP By similarity
Binding site2631IMP By similarity
Binding site3311IMP By similarity
Binding site3331GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TM37 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 7D45BEC2051691FC

FASTA45949,456
        10         20         30         40         50         60 
MQAAIKGRNV VVVGTQWGDE GKGKLVDWLT ESAQGVVRFQ GGHNAGHTLV INGVKTALHL 

        70         80         90        100        110        120 
IPSGIMRPGV KCYIGNGVVL SAAKLFEEIE GLEKAGVEVR SRLRISEACP LILPFHAALD 

       130        140        150        160        170        180 
VAREAAREHG GSEKIGTTGR GIGPAYEDKV ARRALRVQDL KHPERFAAKL KELLALHNHV 

       190        200        210        220        230        240 
LKSFLHSGSF QFGSALQPYL KDGEVQFDAV YQEAMRHAEL LKPMIADVSR ELNEAHKAGA 

       250        260        270        280        290        300 
NLLFEGAQGT LLDVDHGTYP YVTSSNCVAG NAAAGSGVGP GLLHYVLGIT KAYCTRVGGG 

       310        320        330        340        350        360 
PFPTELEWEK PGTPGYHMST IGAEKGVTTG RSRRCGWFDA ALLKRSAQVN GLTGLCITKL 

       370        380        390        400        410        420 
DVLDGLEELK LCVGYELDGE RIDILPMGAE EIARCVPVYE TLAGWSDSTV GVTQYDSLPA 

       430        440        450 
NARRYLERIA EVTAVPIAMI STSPDRDHTI MMQHPYAAQ

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References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000512 Genomic DNA. Translation: ABM32025.1.
RefSeqYP_969799.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TM37.
SMRA1TM37. Positions 7-458.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TM37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4669237.
GenomeReviewsGene locus Aave_1434 in contig CP000512_GR.
KEGGaav:Aave_1434.
NMPDRfig|397945.5.peg.1259.
PATRIC20677934. VBIAciCit38535_1475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0104.
HOGENOMHBG658237.
OMAYVLGIIK.
PhylomeDBA1TM37.
ProtClustDBPRK01117.

Enzyme and pathway databases

BioCycAAVE397945:AAVE_1434-MONOMER.

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 namePURA_ACIAC
AccessionPrimary (citable) accession number: A1TM37
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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