PURA_HELPY
ID PURA_HELPY Reviewed; 411 AA.
AC P56137;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=HP_0255;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07324.1; -; Genomic_DNA.
DR PIR; G64551; G64551.
DR RefSeq; NP_207053.1; NC_000915.1.
DR RefSeq; WP_000796173.1; NC_018939.1.
DR PDB; 6ZXQ; X-ray; 1.40 A; A=1-411.
DR PDBsum; 6ZXQ; -.
DR AlphaFoldDB; P56137; -.
DR SMR; P56137; -.
DR DIP; DIP-3533N; -.
DR IntAct; P56137; 1.
DR MINT; P56137; -.
DR STRING; 85962.C694_01290; -.
DR PaxDb; P56137; -.
DR EnsemblBacteria; AAD07324; AAD07324; HP_0255.
DR KEGG; hpy:HP_0255; -.
DR PATRIC; fig|85962.47.peg.275; -.
DR eggNOG; COG0104; Bacteria.
DR OMA; FHHAKPI; -.
DR PhylomeDB; P56137; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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; Reference proteome.
FT CHAIN 1..411
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000095186"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 11..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 12..15
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 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 37..40
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 39..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 121
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 135
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 215
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 230
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 290..296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 294
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 296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 322..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 400..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT TURN 164..168
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 173..188
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 276..284
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 330..340
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6ZXQ"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:6ZXQ"
SQ SEQUENCE 411 AA; 45743 MW; 7E9D1FCB6A035FB7 CRC64;
MADVVVGIQW GDEGKGKIVD RIAKDYDFVV RYQGGHNAGH TIVHKGVKHS LHLMPSGVLY
PKCKNIISSA VVVSVKDLCE EISAFEDLEN RLFVSDRAHV ILPYHAKKDA FKEKSQNIGT
TKKGIGPCYE DKMARSGIRM GDLLDDKILE EKLNAHFKAI EPFKKAYDLG ENYEKDLMGY
FKTYAPKICP FIKDTTSMLI EANQKGEKIL LEGAQGTLLD IDLGTYPFVT SSNTTSASAC
VSTGLNPKAI NEVIGITKAY STRVGNGPFP SEDTTPMGDH LRTKGAEFGT TTKRPRRCGW
LDLVALKYAC ALNGCTQLAL MKLDVLDGID AIKVCVAYER KGERLEIFPS DLKDCVPIYQ
TFKGWEKSVG VRKLDDLEPN VREYIRFIEK EVGVKIRLIS TSPEREDTIF L
