ID   PUR7_SACD2              Reviewed;         367 AA.
AC   Q21MZ8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Sde_0669;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD79931.1; -; Genomic_DNA.
DR   RefSeq; WP_011467152.1; NC_007912.1.
DR   AlphaFoldDB; Q21MZ8; -.
DR   SMR; Q21MZ8; -.
DR   STRING; 203122.Sde_0669; -.
DR   EnsemblBacteria; ABD79931; ABD79931; Sde_0669.
DR   KEGG; sde:Sde_0669; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_064197_0_0_6; -.
DR   OMA; QKARPVM; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000001947; 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; IPR014106; SAICAR_synthase_Vibrio-typ.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR02735; purC_vibrio; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..367
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000117842"
SQ   SEQUENCE   367 AA;  41284 MW;  D60275ED2C5B1E07 CRC64;
     MSLAHQVLAV NNDLPIRTDK PVHSGKVRSV YWLTAEDSAR LIKEKGYNVA ADAPLAIMVI
     SDRLSAFDCI WHAEGDVRGV PGKGAALNAI SNHWFELFRQ NGLADSHILD IPHPFIWIVQ
     KAKPVMIEAI CRQYITGSMW RAYSKGERNF CGINLEDGLQ KDQKLSELLI TPSTKGILKG
     VPGVPEVDDV NITRADIENN FAAFQFKQKS DIDQYEKLLK EGFNLISGAL EELDQIFVDT
     KFEFGYVTDA SGNDKLIYMD EVGTPDSSRI WDGENYRNGK IIEKSKEGFR QTLLSHFPDP
     DILLNKDRMP ERQALAQDNA LPIDVFMDLS STYLDIAEKI TGQKIVLSEN PKQEIIDILA
     RDFDVII