PURA_BURTA
ID PURA_BURTA Reviewed; 448 AA.
AC Q2SWD3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011};
DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011};
DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011};
DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011};
GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; OrderedLocusNames=BTH_I2245;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC nucleotide biosynthesis. Catalyzes the first committed step in the
CC biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
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_00011};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00011};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00011};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00011}.
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DR EMBL; CP000086; ABC37654.1; -; Genomic_DNA.
DR RefSeq; WP_011402304.1; NZ_CP008785.1.
DR PDB; 3UE9; X-ray; 1.95 A; A/B/C/D=1-448.
DR PDBsum; 3UE9; -.
DR AlphaFoldDB; Q2SWD3; -.
DR SMR; Q2SWD3; -.
DR PRIDE; Q2SWD3; -.
DR EnsemblBacteria; ABC37654; ABC37654; BTH_I2245.
DR GeneID; 66547272; -.
DR KEGG; bte:BTH_I2245; -.
DR HOGENOM; CLU_029848_0_0_4; -.
DR OMA; FHHAKPI; -.
DR OrthoDB; 232152at2; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniPathway.
DR CDD; cd03108; AdSS; 1.
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; IPR033128; Adenylosuccin_syn_Lys_AS.
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 TIGRFAMs; TIGR00184; purA; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..448
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_1000000791"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT ACT_SITE 51
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 22..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 23..26
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_00011"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 48..51
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_00011"
FT BINDING 50..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 139
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_00011"
FT BINDING 153
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 234
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_00011"
FT BINDING 249
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_00011"
FT BINDING 317..323
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 321
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_00011"
FT BINDING 323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 349..351
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 431..433
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 164..184
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3UE9"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 257..262
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 271..282
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:3UE9"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 357..367
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3UE9"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3UE9"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:3UE9"
SQ SEQUENCE 448 AA; 48285 MW; 065A5E765F5E92DA CRC64;
MSASAVNVTP GRNVVVVGTQ WGDEGKGKIV DWLTDHAQGV VRFQGGHNAG HTLIIGGKKT
ILRLIPSGIM REGVACYIGN GVVLSPEALF KEIGELEEAG LSVRERLFIS EATTLILPYH
IAIDQAREAR KGAGKIGTTG RGIGPAYEDK VGRRALRVQD LFDARTFADR LRENLDFHNF
VLTQYLGGAA VDFQATLDTM LGYADRLRPM VADVSRRLYE ENHAGRNLLF EGAQGTLLDI
DHGTYPFVTS SNCVAGAAAA GAGVGPQKLN YILGITKAYC TRVGSGPFPS ELYDADNPSR
QDQIGITLAN VGKEFGSVTG RPRRTGWLDA AALRRSIQIN GVSGLCMTKL DVLDGLDEVK
LCVGYKIDGE DADLLPRGAA EVARCEPVYE TFGGWKESTV GINSWDALPA NARAYLTRVQ
EVAGVPIDMV STGPDRDETI LLRHPFKV
