ID PURA_YERPE Reviewed; 432 AA.
AC Q8ZIV7; Q0WJT2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 148.
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};
GN OrderedLocusNames=YPO0378, y0635, YP_0534;
OS Yersinia pestis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM84223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS60804.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL19060.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84223.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS60804.1; ALT_INIT; Genomic_DNA.
DR PIR; AB0047; AB0047.
DR RefSeq; WP_002209157.1; NZ_WUCM01000083.1.
DR RefSeq; YP_002345456.1; NC_003143.1.
DR PDB; 3HID; X-ray; 1.60 A; A=1-432.
DR PDBsum; 3HID; -.
DR AlphaFoldDB; Q8ZIV7; -.
DR SMR; Q8ZIV7; -.
DR IntAct; Q8ZIV7; 1.
DR STRING; 214092.YPO0378; -.
DR DrugBank; DB02580; Pentaglyme.
DR PaxDb; 214092-YPO0378; -.
DR DNASU; 1145582; -.
DR EnsemblBacteria; AAS60804; AAS60804; YP_0534.
DR GeneID; 66843152; -.
DR KEGG; ype:YPO0378; -.
DR KEGG; ypk:y0635; -.
DR KEGG; ypm:YP_0534; -.
DR PATRIC; fig|214092.21.peg.615; -.
DR eggNOG; COG0104; Bacteria.
DR HOGENOM; CLU_029848_0_0_6; -.
DR OMA; FHHAKPI; -.
DR OrthoDB; 9807553at2; -.
DR UniPathway; UPA00075; UER00335.
DR EvolutionaryTrace; Q8ZIV7; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 1.
DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1.
DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 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 NCBIfam; TIGR00184; purA; 1.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..432
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000095263"
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 5..13
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:3HID"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 155..175
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3HID"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:3HID"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3HID"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3HID"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:3HID"
SQ SEQUENCE 432 AA; 47278 MW; 6A0C351ADC66BF4B CRC64;
MGKNVVVLGT QWGDEGKGKV VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI
LRENVISIIG NGVVLAPDAL MKEMTELEAR GVPVRERLLL SEACPLILPY HVALDNAREK
ARGAKAIGTT GRGIGPAYED KVARRGLRVS DLFNKETFAI KLKEIVEYHN FQLVHYYKEA
AVDYQKVLDD VLAIADILTA MVVDVSELLD NARKQGELIM FEGAQGTLLD IDHGTYPYVT
SSNTTAGGVA TGSGLGPRYV DYVLGIVKAY STRVGAGPFP TELNDETGEF LRKQGNEYGA
TTGRSRRTGW LDIVAVRRAV QINSLSGFCM TKLDVLDGLK EVKLCVGYRM PDGREVDTTP
LAAEGWEGIE PIYETMPGWS ETTFGVKEHS KLPQAALNYI QRVEELTGVP IDIISTGPDR
DETMILRDPF DA
//
