ID   PUR7_CANMA              Reviewed;         291 AA.
AC   P27602;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE            EC=6.3.2.6;
DE   AltName: Full=SAICAR synthetase;
GN   Name=ADE1;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VSB-899;
RX   PubMed=1743515; DOI=10.1016/0378-1119(91)90311-x;
RA   Sasnauskas K., Jomantiene R., Geneviciute E., Januska A., Lebedys J.;
RT   "Molecular cloning of the Candida maltosa ADE1 gene.";
RL   Gene 107:161-164(1991).
RN   [2]
RP   SEQUENCE REVISION.
RA   Sasnauskas K.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977;
RX   PubMed=1368674; DOI=10.1271/bbb1961.55.59;
RA   Kawai S., Hikiji T., Murao S., Takagi M., Yano K.;
RT   "Isolation and sequencing of a gene, C-ADE1, and its use for a host-vector
RT   system in Candida maltosa with two genetic markers.";
RL   Agric. Biol. Chem. 55:59-65(1991).
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   -!- 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   -!- SIMILARITY: Belongs to the SAICAR synthetase family. {ECO:0000305}.
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DR   EMBL; M58322; AAA34318.1; -; Genomic_DNA.
DR   EMBL; D00855; BAA00731.1; -; Genomic_DNA.
DR   PIR; JH0489; JH0489.
DR   PIR; S55291; S55291.
DR   PIR; S55292; S55292.
DR   PIR; S55293; S55293.
DR   AlphaFoldDB; P27602; -.
DR   SMR; P27602; -.
DR   UniPathway; UPA00074; UER00131.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; PS01057; SAICAR_SYNTHETASE_1; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..291
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_0000100924"
SQ   SEQUENCE   291 AA;  32941 MW;  A1DF09E65E9A9117 CRC64;
     MTSTNLEGTF PLIAKGKVRD IYQVDDNTLL FVATDRISAY DVIMSNGIPN KGKILTKLSE
     FWFDFLPIEN HLIKGDIFQK YPQLEPYRNQ LEGRSLLVRK LKLIPLEVIV RGYITGSGWK
     EYQKSKTVHG IPIGDVVESQ QITPIFTPST KAEQGEHDEN ITKEQADKIV GKELCDRIEK
     IAIDLYTKAR DYAATKGIII ADTKFEFGLD GDNIVLVDEV LTPDSSRFWN AAKYEVGKSQ
     DSYDKQFLRD WLTSNGVAGK DGVAMPEDIV TETKSKYVEA YENLTGDKWQ E