ID   PUR71_RHILO             Reviewed;         264 AA.
AC   Q98NM8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase 1;
DE            EC=6.3.2.6;
DE   AltName: Full=SAICAR synthetase 1;
GN   Name=purC1; Synonyms=purC; OrderedLocusNames=mll0069;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB47733.1; -; Genomic_DNA.
DR   RefSeq; WP_010909103.1; NC_002678.2.
DR   AlphaFoldDB; Q98NM8; -.
DR   SMR; Q98NM8; -.
DR   STRING; 266835.14021120; -.
DR   EnsemblBacteria; BAB47733; BAB47733; BAB47733.
DR   GeneID; 66684389; -.
DR   KEGG; mlo:mll0069; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_061495_2_0_5; -.
DR   OMA; EFCYKND; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000000552; 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   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   CDD; cd01415; SAICAR_synt_PurC; 1.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR033934; SAICAR_synt_PurC.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..264
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase 1"
FT                   /id="PRO_0000100859"
SQ   SEQUENCE   264 AA;  29949 MW;  09D03A085FFBB8E9 CRC64;
     MKNRRRIYEG KAKILYEGPE PGTLIQFFKD DATAFNKKKH EVVDGKGVLN NRISEHIFNH
     LNRMGIPTHF IRRLNMREQL IKEVEIIPLE VVVRNVAAGS LSKRLGIEEG TVLPRSIIEF
     YYKADALDDP MVSEEHITAF GWASPQEIDD VMALAIRVND FLSGLFMGVG IQLVDFKIEC
     GRLFEGDMMR IVVADEISPD SCRLWDVATQ DKLDKDRFRR DMGGLVEAYQ EVARRLGIMN
     ENEPPRPTGP VLVASTDVVK GKPH