PURA_BACAN
ID PURA_BACAN Reviewed; 429 AA.
AC Q81JI9; Q6HQ31; Q6KJH5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=BA_5716, GBAA_5716, BAS5320;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP29348.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34877.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57607.1; -; Genomic_DNA.
DR RefSeq; NP_847862.1; NC_003997.3.
DR RefSeq; WP_000100223.1; NZ_WXXJ01000028.1.
DR RefSeq; YP_031557.1; NC_005945.1.
DR PDB; 4M0G; X-ray; 2.15 A; A/B=1-429.
DR PDB; 4M9D; X-ray; 1.82 A; A/B=1-429.
DR PDBsum; 4M0G; -.
DR PDBsum; 4M9D; -.
DR AlphaFoldDB; Q81JI9; -.
DR SMR; Q81JI9; -.
DR IntAct; Q81JI9; 1.
DR STRING; 260799.BAS5320; -.
DR DNASU; 1085481; -.
DR EnsemblBacteria; AAP29348; AAP29348; BA_5716.
DR EnsemblBacteria; AAT34877; AAT34877; GBAA_5716.
DR GeneID; 45025295; -.
DR KEGG; ban:BA_5716; -.
DR KEGG; bar:GBAA_5716; -.
DR KEGG; bat:BAS5320; -.
DR PATRIC; fig|198094.11.peg.5678; -.
DR eggNOG; COG0104; Bacteria.
DR HOGENOM; CLU_029848_0_0_9; -.
DR OMA; FHHAKPI; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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..429
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000095143"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT ACT_SITE 41
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 12..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 13..16
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 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 38..41
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 40..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 128
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 142
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 223
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 238
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 298..304
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 302
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 304
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 330..332
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 412..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4M9D"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:4M9D"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 153..175
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 182..196
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4M9D"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 260..275
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:4M9D"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 391..404
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:4M9D"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:4M9D"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:4M9D"
SQ SEQUENCE 429 AA; 47424 MW; 0E44D5BA065649D5 CRC64;
MSSVVVVGTQ WGDEGKGKIT DFLSEHAEVV ARYQGGNNAG HTIVFGGVKY KLHLIPSGIF
YKEKICVIGN GLVVDPKALL EELKYLHDRG VSTDNLRVSN RAHVILPYHL KQDELEEASK
GDNKIGTTKK GIGPAYMDKA ARIGIRMADL LDREAFKEKL EQNLAQKNRL FEKMYDTEGF
SVDEIFEEYF EYGQQIAQYV CDTSVVLNDA LDNNHRVLFE GAQGVMLDID HGTYPFVTSS
NPIAGGVTVG TGVGPAKVTR VVGVCKAYTS RVGDGPFPTE LHDEIGHQIR EVGREYGTTT
GRPRRVGWFD SVVVRHARRV SGLTDLSLNS IDVLTGIPTL KICVAYKCDG KVIDEVPANL
NILAKCEPVY EELPGWTEDI TGVRSLDELP ENARKYVERV SELTGIQLSM FSVGPDRNQT
NIVRNVYEA
