PURA_LEIMA
ID PURA_LEIMA Reviewed; 710 AA.
AC Q4QG35;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03125};
DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_03125};
DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_03125};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03125};
DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_03125};
GN ORFNames=LmjF13.1190, LmjF_13_1190;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
CC -!- FUNCTION: Plays an important role in the salvage pathway for purine
CC nucleotide biosynthesis. Catalyzes the first committed step in the
CC biosynthesis of AMP from IMP (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03125};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03125};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03125}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03125}.
CC -!- MISCELLANEOUS: Parasitic protozoa lack the de novo purine biosynthesis
CC pathway and rely exclusively on the salvage pathway for their purine
CC nucleotide requirements.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03125}.
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DR EMBL; FR796409; CAJ03014.1; -; Genomic_DNA.
DR RefSeq; XP_001681863.1; XM_001681811.1.
DR AlphaFoldDB; Q4QG35; -.
DR SMR; Q4QG35; -.
DR STRING; 5664.LmjF.13.1190; -.
DR PRIDE; Q4QG35; -.
DR EnsemblProtists; CAJ03014; CAJ03014; LMJF_13_1190.
DR GeneID; 5650148; -.
DR KEGG; lma:LMJF_13_1190; -.
DR VEuPathDB; TriTrypDB:LmjF.13.1190; -.
DR VEuPathDB; TriTrypDB:LMJLV39_130016100; -.
DR VEuPathDB; TriTrypDB:LMJSD75_130016100; -.
DR eggNOG; KOG1355; Eukaryota.
DR InParanoid; Q4QG35; -.
DR OMA; HHGECGA; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000000542; Chromosome 13.
DR GO; GO:0097014; C:ciliary plasm; ISO:GeneDB.
DR GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR Gene3D; 3.90.170.10; -; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..710
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000399304"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 180..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 181..184
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 208..211
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 210..212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 295
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 309
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 421
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 437
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 563..569
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 567
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 569
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
FT BINDING 697..699
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03125"
SQ SEQUENCE 710 AA; 78272 MW; 5491E333F2432DCD CRC64;
MPVRRYGGRY NSSSPGVSNA LNPSRTAGWP LSPSPATGSK PASTHHDPVP QEAYYVKDEA
DARHQQQAPL REPSVEVEVE IIDDEPPRGS QKPLSVAPCT ANANNSSGGS KCNAITASRY
TFYTNAYQKS VYEALRSLRP LPELQEPRRV KEYAETSLKD SLYRIVEAHD VIMVAGAFFG
DEGKGKTVDA VARHPLCTCI ARVNSGENAG HTVYDKAGRK FVFNLAPSGL LLPGKRNYIG
PECVMDPVSF MEKEVIQLID AGIDYRDRLF IGNVCIVTPY HKLLDLLGSA ANSSTLKGMA
PVHGSKVMKR GIRLDHIFND DETLRKRLEK DMDTYFGLLK VKNLSDADVV RLCREENSDG
VVRVPDYVIA FAQAEDKVEF LVKLYRDRVR HNPGFPARCD VTYELHAALL RGEKVLLEGP
QSYWLSNART KFWESTTSAD TTAAGLLAAS QLNFQKFKSV VLNVHKAPGS SRVGIGACPS
SFVPQDYFSA QNIKTLRDLP SATCAHFEAV QRTLFRDGFP HSNDKARHNG IMAPVEYSDE
TGTYNIGVAM AIASAQHHGE CGAVTKKPRV CGFFDCVLHH EVNNIQGPYL TISALDRGDE
YDKVGVTIAY VYYSPEGKQV DVNGHVYKNG DIIRAGDPVP SEPALYHCHP IVKLIDGWRD
NPIAAAKRRR NAPLPRGVCE LLSAIEYFTN CKILSIGNGP NGDDIIYLRQ
