ID   PUR7_ACIF5              Reviewed;         240 AA.
AC   B5ELM2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-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=Lferr_1989;
OS   Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS   (Leptospirillum ferrooxidans (ATCC 53993)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53993 / BNL-5-31;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Borole A.P.;
RT   "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL   Submitted (AUG-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; CP001132; ACH84206.1; -; Genomic_DNA.
DR   RefSeq; WP_012537146.1; NC_011206.1.
DR   AlphaFoldDB; B5ELM2; -.
DR   SMR; B5ELM2; -.
DR   GeneID; 66433333; -.
DR   KEGG; afe:Lferr_1989; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_061495_2_0_6; -.
DR   OMA; EFCYKND; -.
DR   UniPathway; UPA00074; UER00131.
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.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..240
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000095961"
SQ   SEQUENCE   240 AA;  27236 MW;  F80951EA302BE3CE CRC64;
     MNERIALYEG KAKIVYASES PDELVLHFKD DTSAFDGEKV EQLAHKGEIN NAFNAFIMEY
     LQGEGVPTHF IRRLNARESL VRRLEMIPVE CVVRNRAAGS LSKRLGIEEG RVLEPPTLEF
     FLKNDALHDP MINTSHIRTF GWATAEEVEA MRRWTMRVNM LLSALFAKAN LILVDFKLEF
     GRFDGELYLG DEFSPDGCRL WDALSLEKMD KDRFRRGLGG VVEAYAEVAR RLGVPLPAAS