PURA_PYRHO
ID PURA_PYRHO Reviewed; 339 AA.
AC O58187;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=PH0438;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of hypothetical adenylosuccinate synthetase, PH0438 from
RT Pyrococcus horikoshii OT3.";
RL Submitted (MAY-2006) to the PDB data bank.
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; BA000001; BAA29524.1; -; Genomic_DNA.
DR PIR; G71154; G71154.
DR RefSeq; WP_010884548.1; NC_000961.1.
DR PDB; 2D7U; X-ray; 2.50 A; A=1-339.
DR PDB; 5K7X; X-ray; 2.80 A; A/B/C/D/E/F=1-339.
DR PDBsum; 2D7U; -.
DR PDBsum; 5K7X; -.
DR AlphaFoldDB; O58187; -.
DR SMR; O58187; -.
DR STRING; 70601.3256841; -.
DR EnsemblBacteria; BAA29524; BAA29524; BAA29524.
DR GeneID; 1444335; -.
DR KEGG; pho:PH0438; -.
DR eggNOG; arCOG04387; Archaea.
DR OMA; FHHAKPI; -.
DR OrthoDB; 35648at2157; -.
DR BRENDA; 6.3.4.4; 5244.
DR UniPathway; UPA00075; UER00335.
DR EvolutionaryTrace; O58187; -.
DR Proteomes; UP000000752; 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; -; 2.
DR Gene3D; 3.90.170.10; -; 2.
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; 3.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 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.
FT CHAIN 1..339
FT /note="Adenylosuccinate synthetase"
FT /id="PRO_0000095277"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT ACT_SITE 43
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 40..43
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 42..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 127
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 141
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 179
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 194
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 252..258
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 256
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 258
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 284..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT BINDING 324..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2D7U"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:5K7X"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5K7X"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:2D7U"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2D7U"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:2D7U"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:2D7U"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:2D7U"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2D7U"
SQ SEQUENCE 339 AA; 37232 MW; ADA2FB1D07CCF3D0 CRC64;
MPSVIVVGGQ WGDEGKGSIV AYLSLHDEPE IIARGGVGTN AGHSVVINGK KYAVRQIPTG
FMQTKARLLI GAGVLVDPEV FFHELEQLKD FNVKDRVGID YRCAIIEEKH KQLDRTNGYL
HGKIGTTGSG CGPANADRVM RKAKQAKDVK ELEPYLTDVA QEINDALDEG SLVLVEGTQG
FGLSLYYGTY PYVTSKDVTA SSVAADVGIG PTRVDEVIVV FKSFPTRVGA GPFPTEMPME
EADRLGLVEY GTVTGRRRRV GWFDFEMARY SARINGATML AVTMLDKYDK EAFGVTDYDK
LPRKAKEFIE EIEERVGVPV GLIKTGPELE HIIDRRDTI
