PURA_THET8
ID PURA_THET8 Reviewed; 408 AA.
AC Q5SLS1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=TTHA0222;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-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; AP008226; BAD70045.1; -; Genomic_DNA.
DR RefSeq; WP_011174122.1; NC_006461.1.
DR RefSeq; YP_143488.1; NC_006461.1.
DR PDB; 6JRQ; X-ray; 2.10 A; A/B/C/D=1-408.
DR PDBsum; 6JRQ; -.
DR AlphaFoldDB; Q5SLS1; -.
DR SMR; Q5SLS1; -.
DR STRING; 300852.55771604; -.
DR EnsemblBacteria; BAD70045; BAD70045; BAD70045.
DR GeneID; 3168479; -.
DR KEGG; ttj:TTHA0222; -.
DR PATRIC; fig|300852.9.peg.220; -.
DR eggNOG; COG0104; Bacteria.
DR HOGENOM; CLU_029848_0_0_0; -.
DR OMA; FHHAKPI; -.
DR PhylomeDB; Q5SLS1; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000000532; 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; 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.
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..408
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000224332"
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 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 213
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 228
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 288..294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 292
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 294
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 320..322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 393..395
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:6JRQ"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:6JRQ"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:6JRQ"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:6JRQ"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:6JRQ"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:6JRQ"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:6JRQ"
SQ SEQUENCE 408 AA; 44879 MW; 2CD58DD49FECDFA8 CRC64;
MPGIAIIGAQ WGDEGKGKVV DVLAREADYV IRYQGGANAG HTVVAEGKVF KLNLLPSGVI
HPHAVNVLGD GMVIDPFRFQ EEVEGLRKEG FDPKILVSER AHLVLPHHKH VESRHNFVGT
TGRGIGPAYS DRARRVGIRA GDLLDEATLR ERVRRLLAEK PNSTREAGWD TEEKALADLH
RMREILSPYI ADTGSLLREA WRKGKRLLFE GAQATLLDLN YGTYPYVTSS HPTVGGILVG
TGLSHKAITK VYGVAKAYTT RVGEGPFPTE LQGELAHHLR EKGGEYGTTT GRPRRVGWLD
LVALRYACEV NGFDGLVLTK LDVLSGLEKV KVAVEYLDGA RPGEASPEAV RYLELPGWGD
LSHVKRREDL PANLLRYLEL VEEHTGVPVV LFSTSPRRED TFGAVSWV
