(data stored in ACNUC7421 zone)

SWISSPROT: PURA_HISS2

ID   PURA_HISS2              Reviewed;         432 AA.
AC   B0UW92;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 69.
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=HSM_0287;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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}.
DR   EMBL; CP000947; ACA31917.1; -; Genomic_DNA.
DR   RefSeq; WP_012341154.1; NC_010519.1.
DR   SMR; B0UW92; -.
DR   EnsemblBacteria; ACA31917; ACA31917; HSM_0287.
DR   GeneID; 31486569; -.
DR   KEGG; hsm:HSM_0287; -.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; FHHAKPI; -.
DR   OrthoDB; 232152at2; -.
DR   BioCyc; HSOM228400:G1GB8-301-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000008543; 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   3: Inferred from homology;
DR   PRODOM; B0UW92.
DR   SWISS-2DPAGE; B0UW92.
KW   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_1000073949"
FT   NP_BIND         13..19
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         41..43
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         332..334
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   NP_BIND         415..417
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          14..17
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          39..42
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   REGION          300..306
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
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   METAL           14
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   METAL           41
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         130
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         144
FT                   /note="IMP; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         225
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         240
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         304
FT                   /note="IMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
FT   BINDING         306
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00011"
SQ   SEQUENCE   432 AA;  47141 MW;  2C84C43084BE4C6A CRC64;
     MGKSVVVLGA QWGDEGKGKI VDLLTDRVKY VVRYQGGHNA GHTLIINGEK TVLRLIPSGI
     LRENVTCLIG NGVVLSPTAL MQEMGELESR GINVRERLLI SEACPLILPY HVAMDKARES
     ALGNKAIGTT GRGIGPAYED KVARRGLRVG DLFDKQSFAE KLKNILDYYN FQLVNYYKVE
     AVDYQKTLDE VLAVADIITA MVADVTTILD VARKNGDNIL FEGAQGTMLD IDQGTYPYVT
     SSNTTAGGVS TGAGFGPRHI DYVLGIIKAY CTRVGGGPFT TELFDEVGAE IARKGNEFGA
     VTGRPRRCGW FDAVAIKRAI QTNSISGFCM TKLDVLDGFR EVKICVGYKM PNGEIAEYAP
     LAAKDWEGVE PIYETLPGWQ ENTFGITDVN QLPENTRNYI KRIEEVTGVP IAILSTGPDR
     VETMILNDPF AV
//

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