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Protein

Adenylosuccinate synthetase

Gene

purA

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: -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.UniRule annotation

Catalytic activityi

GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from IMP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase (purA)
  2. Adenylosuccinate lyase (purB)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei13Proton acceptorUniRule annotation1
Metal bindingi13MagnesiumUniRule annotation1
Metal bindingi40Magnesium; via carbonyl oxygenUniRule annotation1
Active sitei41Proton donorUniRule annotation1
Binding sitei129IMPUniRule annotation1
Binding sitei143IMP; shared with dimeric partnerUniRule annotation1
Binding sitei224IMPUniRule annotation1
Binding sitei239IMPUniRule annotation1
Binding sitei303IMPUniRule annotation1
Binding sitei305GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 18GTPUniRule annotation7
Nucleotide bindingi40 – 42GTPUniRule annotation3
Nucleotide bindingi331 – 333GTPUniRule annotation3
Nucleotide bindingi413 – 415GTPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processPurine biosynthesis
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMLEP272631:G1GT5-317-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:ML0280
ORF Names:MLCB4.23c
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0280

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000951981 – 432Adenylosuccinate synthetaseAdd BLAST432

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272631.ML0280

Structurei

3D structure databases

ProteinModelPortaliO69595
SMRiO69595
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 16IMP bindingUniRule annotation4
Regioni38 – 41IMP bindingUniRule annotation4
Regioni299 – 305Substrate bindingUniRule annotation7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C91 Bacteria
COG0104 LUCA
HOGENOMiHOG000260959
KOiK01939
OMAiSNAGHTV
OrthoDBiPOG091H01G9

Family and domain databases

CDDicd03108 AdSS, 1 hit
HAMAPiMF_00011 Adenylosucc_synth, 1 hit
InterProiView protein in InterPro
IPR018220 Adenylosuccin_syn_GTP-bd
IPR033128 Adenylosuccin_syn_Lys_AS
IPR001114 Adenylosuccinate_synthetase
IPR027417 P-loop_NTPase
PANTHERiPTHR11846 PTHR11846, 1 hit
PfamiView protein in Pfam
PF00709 Adenylsucc_synt, 1 hit
SMARTiView protein in SMART
SM00788 Adenylsucc_synt, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00184 purA, 1 hit
PROSITEiView protein in PROSITE
PS01266 ADENYLOSUCCIN_SYN_1, 1 hit
PS00513 ADENYLOSUCCIN_SYN_2, 1 hit

Sequencei

Sequence statusi: Complete.

O69595-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAVVLIGAQ WGDEGKGKVT DLLGGRAQWV VRYQGGNNAG HTVVLPTGEN
60 70 80 90 100
FTLHLIPSGV LTPGVTNVIG NGVVVDPGVL LSELQGLEDR GVDTSQLLIS
110 120 130 140 150
ADAHLLMPYH VAIDKVTERY MGNKKIGTTG RGIGPCYQDK IARMGIRVAD
160 170 180 190 200
VLEPGELTHK IEAALEFKNQ VLVKIYNRKA LDLAQVVETL LEQAQQFRHR
210 220 230 240 250
ITDTRLLLND ALEAGETVLL EGAQGTLLDV DHGTYPYVTS SNPTAGGAAL
260 270 280 290 300
GSGIGPTRIH TVLGILKAYT TRVGSGPFPT ELFDENGEYL AKTGSEIGVT
310 320 330 340 350
TGRRRRCGWF DAVIARYATR VNGITDYFLT KLDVLSSLET VPVCVGYQIA
360 370 380 390 400
GVRTHDMPIT QSDLARAEPI YEELPGWWED ISGAREFEDL PAKARDYVLR
410 420 430
LEELAGAQVA CIGVGPGRDQ TIVRCDVLRS RR
Length:432
Mass (Da):46,793
Last modified:August 1, 1998 - v1
Checksum:iC6D75C5D2580C5F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL023514 Genomic DNA Translation: CAA18944.1
AL583918 Genomic DNA Translation: CAC29788.1
PIRiH86943
RefSeqiNP_301321.1, NC_002677.1
WP_010907645.1, NC_002677.1

Genome annotation databases

EnsemblBacteriaiCAC29788; CAC29788; CAC29788
GeneIDi908815
KEGGimle:ML0280
PATRICifig|272631.5.peg.444

Similar proteinsi

Entry informationi

Entry nameiPURA_MYCLE
AccessioniPrimary (citable) accession number: O69595
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: March 28, 2018
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health