ID   PUR72_RHILO             Reviewed;         313 AA.
AC   Q98I23;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Putative phosphoribosylaminoimidazole-succinocarboxamide synthase 2;
DE            EC=6.3.2.6;
DE   AltName: Full=SAICAR synthetase 2;
GN   Name=purC2; OrderedLocusNames=mll2603;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB49693.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000012; BAB49693.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044548260.1; NC_002678.2.
DR   AlphaFoldDB; Q98I23; -.
DR   SMR; Q98I23; -.
DR   STRING; 266835.14023086; -.
DR   EnsemblBacteria; BAB49693; BAB49693; BAB49693.
DR   KEGG; mlo:mll2603; -.
DR   PATRIC; fig|266835.9.peg.2089; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_045637_0_1_5; -.
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   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 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..313
FT                   /note="Putative phosphoribosylaminoimidazole-
FT                   succinocarboxamide synthase 2"
FT                   /id="PRO_0000100860"
SQ   SEQUENCE   313 AA;  35091 MW;  D1FB00CB54256D2E CRC64;
     MRTLSDAFIP ELPGYYKGKV RENYDLADGR RIIIATDRLS AFDIILTSIP FKGEILTQTA
     RYWFEETADI CPNHVLEYPD PNVVVGTRLD ILPVEIVVRG YLAGTTSTSI LTRYRRGERE
     MYGMRLPDGL RDNEKLAAPV ITPTSKAADG GHDEPLSRAE ILAQGLLTQA QWDTVSDYAL
     KLFARGQARA AERGLILADT KYEFGTDKNG TIILADEIHT PDSSRYWIAA SYEQALASGT
     RPDSFDKDFI RSWVAARCDP YKDPIPRIPD EIVEQASRIY AQAYEAITGK AFVPDLSGDT
     VLDRIRSNLV RFF