ID   PUR7_ELUMP              Reviewed;         292 AA.
AC   B2KCE9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000255|HAMAP-Rule:MF_00137};
DE            EC=6.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00137};
DE   AltName: Full=SAICAR synthetase {ECO:0000255|HAMAP-Rule:MF_00137};
GN   Name=purC {ECO:0000255|HAMAP-Rule:MF_00137}; OrderedLocusNames=Emin_0514;
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191;
RX   PubMed=19270133; DOI=10.1128/aem.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC         L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC         4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC         ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00137};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00137}.
CC   -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00137}.
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DR   EMBL; CP001055; ACC98070.1; -; Genomic_DNA.
DR   RefSeq; WP_012414685.1; NC_010644.1.
DR   AlphaFoldDB; B2KCE9; -.
DR   SMR; B2KCE9; -.
DR   STRING; 445932.Emin_0514; -.
DR   EnsemblBacteria; ACC98070; ACC98070; Emin_0514.
DR   KEGG; emi:Emin_0514; -.
DR   HOGENOM; CLU_045637_0_2_0; -.
DR   OMA; TKFEFGF; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000001029; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR001636; SAICAR_synth.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR00081; purC; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..292
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000122916"
SQ   SEQUENCE   292 AA;  32826 MW;  3311DAC625154DE0 CRC64;
     MNNSQINLPL LKKGKVRDVY DAGKMLLIVA SDRVSVFDCV LPSQIPDKGK ILTQISNFWF
     AKTISIVPNH MISSDINEIN IILKLGLDPQ YYSGRTVLVK KCERIDFECV VRGYITGSAW
     KEYQKSGTVC GEKIKEGLKE AQKFPEPIFT PASKADTGHD ENVSFAYMLS HMDKNLAYKI
     KDTSIKLYNF AEEYLKNCGI ILADTKFEFG LIDGDLILID EILTPDSSRF WDAALYKTGT
     NPPGFDKQFV RDYMEQTGWD KNPPPPAMPQ SIALAAAKKY KEALSRIEKG SV