ID   PUR7_STRM5              Reviewed;         308 AA.
AC   B4SLF7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Smal_3727;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF53426.1; -; Genomic_DNA.
DR   RefSeq; WP_006399041.1; NC_011071.1.
DR   AlphaFoldDB; B4SLF7; -.
DR   SMR; B4SLF7; -.
DR   STRING; 391008.Smal_3727; -.
DR   EnsemblBacteria; ACF53426; ACF53426; Smal_3727.
DR   KEGG; smt:Smal_3727; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_045637_0_2_6; -.
DR   OMA; TKFEFGF; -.
DR   BioCyc; SMAL391008:SMAL_RS18930-MON; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000001867; 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; 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..308
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000096019"
SQ   SEQUENCE   308 AA;  34149 MW;  D9298377CBC336E6 CRC64;
     MPTTLLQSDL PGLPLRHRGK VRDVFDIPRE RLPAGTPPGD YLLMVATDRL SAFDVVLPDP
     IPGKGEMLCQ VSNFWFAKTA HLMPNHLTGI DVASVLPEGV DPALYAKRAV VTRKLKPVPV
     EAIARGYLIG SGWKDYQRTG KVSGIDLPDG LRQAEQLPEP IFTPSTKAAV GDHDENIDFD
     AMVKQVGAEM AERVRDATLR IYKFAADYAR ERGIILADTK FEFGTDADGR LYIMDEMLTP
     DSSRYWPADE YEVGTSPPSY DKQFVRDYLE TLDWGKTAPG PTIPAEIIER TRAKYGEALQ
     RLAGISVD