(data stored in ACNUC7421 zone)

SWISSPROT: PURA1_PSEHT

ID   PURA1_PSEHT             Reviewed;         437 AA.
AC   Q3IEZ3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 85.
DE   RecName: Full=Adenylosuccinate synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00011};
DE            Short=AMPSase 1 {ECO:0000255|HAMAP-Rule:MF_00011};
DE            Short=AdSS 1 {ECO:0000255|HAMAP-Rule:MF_00011};
DE            EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011};
DE   AltName: Full=IMP--aspartate ligase 1 {ECO:0000255|HAMAP-Rule:MF_00011};
GN   Name=purA1 {ECO:0000255|HAMAP-Rule:MF_00011};
GN   OrderedLocusNames=PSHAa0275;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-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-
CC       Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP 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; CR954246; CAI85374.1; -; Genomic_DNA.
DR   RefSeq; WP_011326988.1; NC_007481.1.
DR   ProteinModelPortal; Q3IEZ3; -.
DR   SMR; Q3IEZ3; -.
DR   STRING; 326442.PSHAa0275; -.
DR   PRIDE; Q3IEZ3; -.
DR   EnsemblBacteria; CAI85374; CAI85374; PSHAa0275.
DR   KEGG; pha:PSHAa0275; -.
DR   PATRIC; fig|326442.8.peg.262; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; GVSKAYT; -.
DR   OrthoDB; POG091H01G9; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03108; AdSS; 1.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR   InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
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; Q3IEZ3.
DR   SWISS-2DPAGE; Q3IEZ3.
KW   Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    437       Adenylosuccinate synthetase 1.
FT                                /FTId=PRO_0000224305.
FT   NP_BIND      13     19       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND      41     43       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND     338    340       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   NP_BIND     421    423       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   REGION       14     17       IMP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   REGION       39     42       IMP binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   REGION      306    312       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     14     14       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     42     42       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   METAL        14     14       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00011}.
FT   METAL        41     41       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     130    130       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     144    144       IMP; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     225    225       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     240    240       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     310    310       IMP. {ECO:0000255|HAMAP-Rule:MF_00011}.
FT   BINDING     312    312       GTP. {ECO:0000255|HAMAP-Rule:MF_00011}.
SQ   SEQUENCE   437 AA;  47120 MW;  70B76AC4238B6964 CRC64;
     MGKNVVVLGT QWGDEGKGKV VDLLTDKASL VVRYQGGHNA GHTLVIDGEK TVLHLIPSGV
     LRDNVKCVIG NGVVLSPEAL MREIGMLEAR GVPVRERLLI SAACPLILPF HVALDVARET
     ARGDKPIGTT GRGIGPAYED KVARRGLRVG DLFNPELFAA KLEEVLEYHN FTLVNYYKVD
     AVDFQKTFDD AMAVADILKA MIVDVTELLD QTRLAGDNIL FEGAQGTLLD IDHGTYPYVT
     SSNTTAGGVA TGAGFGPLHL DYVLGIIKAY TTRVGSGPFP TELYDGLDKQ DPVGKHLGDK
     GHEFGATTGR LRRTGWLDAV AMRRAVQINS ISGFCLTKLD VLDGLETLKI CTGYKLEDGT
     VTNVTPLAAE GYEKVTPIYE EMPGWSENTV GVTSLDGLPK AAIDYVKRIE ELTGVPVDII
     STGPDRVETM ILRNPFA
//

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