ID   D0JBF3_BLASB            Unreviewed;       242 AA.
AC   D0JBF3;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000256|HAMAP-Rule:MF_00137};
DE            EC=6.3.2.6 {ECO:0000256|HAMAP-Rule:MF_00137};
DE   AltName: Full=SAICAR synthetase {ECO:0000256|HAMAP-Rule:MF_00137};
GN   Name=purC {ECO:0000256|HAMAP-Rule:MF_00137,
GN   ECO:0000313|EMBL:ACY40491.1};
GN   OrderedLocusNames=BLBBGE_484 {ECO:0000313|EMBL:ACY40491.1};
OS   Blattabacterium sp. subsp. Blattella germanica (strain Bge) (Blattella
OS   germanica symbiotic bacterium).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=331104 {ECO:0000313|EMBL:ACY40491.1, ECO:0000313|Proteomes:UP000002625};
RN   [1] {ECO:0000313|EMBL:ACY40491.1, ECO:0000313|Proteomes:UP000002625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bge {ECO:0000313|Proteomes:UP000002625};
RX   PubMed=19911043; DOI=10.1371/journal.pgen.1000721;
RA   Lopez-Sanchez M.J., Neef A., Pereto J., Patino-Navarrete R., Pignatelli M.,
RA   Latorre A., Moya A.;
RT   "Evolutionary convergence and nitrogen metabolism in Blattabacterium strain
RT   Bge, primary endosymbiont of the cockroach Blattella germanica.";
RL   PLoS Genet. 5:E1000721-E1000721(2009).
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:0000256|ARBA:ARBA00000706, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00004672, ECO:0000256|HAMAP-Rule:MF_00137}.
CC   -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC       {ECO:0000256|ARBA:ARBA00010190, ECO:0000256|HAMAP-Rule:MF_00137}.
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DR   EMBL; CP001487; ACY40491.1; -; Genomic_DNA.
DR   RefSeq; WP_012841006.1; NC_013454.1.
DR   AlphaFoldDB; D0JBF3; -.
DR   STRING; 331104.BLBBGE_484; -.
DR   KEGG; bbl:BLBBGE_484; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_061495_2_0_10; -.
DR   OrthoDB; 9801549at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000002625; 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   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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   NCBIfam; TIGR00081; purC; 1.
DR   PANTHER; PTHR43599:SF3; BIFUNCTIONAL PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE_PHOSPHORIBOSYLAMINOIMIDAZOLE SUCCINOCARBOXAMIDE SYNTHETASE; 1.
DR   PANTHER; PTHR43599; MULTIFUNCTIONAL PROTEIN ADE2; 1.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00137};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00137};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00137};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00137}.
FT   DOMAIN          10..228
FT                   /note="SAICAR synthetase/ADE2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01259"
SQ   SEQUENCE   242 AA;  28366 MW;  127ECE303EECB463 CRC64;
     MSFVIKKNLL SEGKTKKIYT TNNSLEVLIH YKDSITALDG SKNQFLQDKG ILNNEISTLI
     FKFINSCGIK THFIRKINNR EQLCYKVDII PLEFVVRNIV AGSMSKRLNI QEGIRLLNPI
     FEIFYKNDKL KDPLINDHHA VFLGIISYEE INAIYRIVSN VNNILKKYFL DKNIILVDFK
     IEFGKNDQND ILLSDEISPD TCRFWDKKTM KKLDKDPFRI GLKEKEEVLD IYMEILKRLN
     VR
//