PURA_LEGPN
ID PURA_LEGPN Reviewed; 431 AA.
AC Q8RNM2;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
OS Legionella pneumophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=446;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12065505; DOI=10.1128/iai.70.7.3637-3648.2002;
RA Rankin S., Li Z., Isberg R.R.;
RT "Macrophage-induced genes of Legionella pneumophila: protection from
RT reactive intermediates and solute imbalance during intracellular growth.";
RL Infect. Immun. 70:3637-3648(2002).
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; AF480918; AAM00648.1; -; Genomic_DNA.
DR RefSeq; WP_010946234.1; NZ_UGOV01000002.1.
DR PDB; 6BS7; X-ray; 1.95 A; A=1-431.
DR PDB; 6C25; X-ray; 1.90 A; A=1-431.
DR PDBsum; 6BS7; -.
DR PDBsum; 6C25; -.
DR AlphaFoldDB; Q8RNM2; -.
DR SMR; Q8RNM2; -.
DR STRING; 91892.BIZ52_02695; -.
DR GeneID; 66489680; -.
DR eggNOG; COG0104; Bacteria.
DR OrthoDB; 232152at2; -.
DR UniPathway; UPA00075; UER00335.
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..431
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000095190"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT ACT_SITE 42
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 13..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 14..17
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 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 39..42
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 41..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 130
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 144
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 225
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 240
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 300..306
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 304
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 306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 332..334
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 415..417
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:6C25"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 155..174
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:6C25"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:6C25"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:6C25"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6C25"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:6C25"
SQ SEQUENCE 431 AA; 47381 MW; D446C19AED550774 CRC64;
MGKNVVVLGT QWGDEGKGKI VDLLTQDAQV VVRYQGGHNA GHTLKINGVK TVLRLIPSGM
LRPNVTCYIA NGVVLSPQAL LSEIKELEGN GINVRERLRI SLACPLILPY HIALDKARET
HMGKSAIGTT GRGIGPAYED KVARRALRVG DLFHRDRFAN KLTELLDYHN FVLTQYFKQP
AVDLESLLGE SLQWAEELRP MVCDVSACLH EHRKQGENIL FEGAQGVYLD IDHGTYPYVT
SSNTCVGSVI NGAGFGPRYI DYVLGITKAY TTRVGGGPFP TELLDDVGKR IAERGQEFGA
VTGRPRRCGW FDAVLLKRSI ELNSISGLCV TKLDVLDGLE VLRIAVAYKD RDGNILSRPP
LAADDFNDLL PVYEELPGWQ ESTADVTVMS DLPANARAYL KRIEEILGIP IDMLSTGPER
DSTITLRGPF L
