PURA_CAMJE
ID PURA_CAMJE Reviewed; 416 AA.
AC Q9PMG4; Q0P8B9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=Cj1498c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL111168; CAL35605.1; -; Genomic_DNA.
DR PIR; G81296; G81296.
DR RefSeq; WP_002851458.1; NC_002163.1.
DR RefSeq; YP_002344878.1; NC_002163.1.
DR PDB; 3R7T; X-ray; 2.30 A; A=1-416.
DR PDBsum; 3R7T; -.
DR AlphaFoldDB; Q9PMG4; -.
DR SMR; Q9PMG4; -.
DR STRING; 192222.Cj1498c; -.
DR PaxDb; Q9PMG4; -.
DR PRIDE; Q9PMG4; -.
DR EnsemblBacteria; CAL35605; CAL35605; Cj1498c.
DR GeneID; 905786; -.
DR KEGG; cje:Cj1498c; -.
DR PATRIC; fig|192222.6.peg.1478; -.
DR eggNOG; COG0104; Bacteria.
DR HOGENOM; CLU_029848_0_0_7; -.
DR OMA; FHHAKPI; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000000799; Chromosome.
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; Reference proteome.
FT CHAIN 1..416
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000095160"
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 126
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 140
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 220
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 235
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 295..301
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 299
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 301
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 327..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 405..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:3R7T"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3R7T"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 255..272
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:3R7T"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 335..345
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:3R7T"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:3R7T"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3R7T"
SQ SEQUENCE 416 AA; 46124 MW; 8EA47E95AD1E919B CRC64;
MSKADIIVGI QWGDEGKGKV VDKLCENYDF VCRSAGGHNA GHTIWVNGVR YALHLMPSGV
LHPRCINIIG NGVVVSPEVL IAEMAQFENL KGRLYISDRA HLNLKHHSLI DIAKEKLKGK
NAIGTTGKGI GPSYADKINR TGHRVGELLE PQRLCEALIK DFEANKTFFE MLEIEIPSAE
ELLADLKRFN EILTPYITDT TRMLWKALDE DKRVLLEGAQ GSMLDIDHGT YPYVTSSSTI
SAGTLTGLGL NPKEAGNIIG IVKAYATRVG NGAFPTEDKG EDGEKIAQIG KEIGVSTGRK
RRCGWFDAVA VRYTARLNGL DALSLMKLDV LDGFEKIKIC RAYEYKGMEI DYIPSDLENV
QPIYEEMDGW DKVFGIKDYD LLPENAKKYI ARLEELAGVK VKYISTSPER DDTIIL
