PUR7_CLOP1
ID PUR7_CLOP1 Reviewed; 235 AA.
AC Q0TTB4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=CPF_0673;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000246; ABG83396.1; -; Genomic_DNA.
DR RefSeq; WP_003456948.1; NC_008261.1.
DR PDB; 3NUA; X-ray; 1.40 A; A/B=1-235.
DR PDBsum; 3NUA; -.
DR AlphaFoldDB; Q0TTB4; -.
DR SMR; Q0TTB4; -.
DR STRING; 195103.CPF_0673; -.
DR EnsemblBacteria; ABG83396; ABG83396; CPF_0673.
DR GeneID; 29572203; -.
DR KEGG; cpf:CPF_0673; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_061495_2_0_9; -.
DR OMA; EFCYKND; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR EvolutionaryTrace; Q0TTB4; -.
DR Proteomes; UP000001823; 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.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..235
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000018692"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3NUA"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3NUA"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:3NUA"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:3NUA"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3NUA"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3NUA"
FT HELIX 146..168
FT /evidence="ECO:0007829|PDB:3NUA"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 172..184
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3NUA"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3NUA"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3NUA"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3NUA"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:3NUA"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:3NUA"
SQ SEQUENCE 235 AA; 27003 MW; 3A41A843F0D61F96 CRC64;
MVNQLEMLYE GKAKKIYATD KEDMVIVHYK DDATAFNGEK KAQIESKGVL NNEITSLIFE
MLNKEGIKTH FVEKLNDRDQ LCKKVEIVPL EVIVRNVAAG SMAKRLGLEE GYELKTTVFE
LSYKDDSLGD PLINDYHAVG IGATTFEELN KIYEITAKVN EILKEAFKKQ NINLIDFKLE
FGRYNGEILL ADEISPDTCR FWDATTGEKM DKDRFRRDMG NVINGYREVL NRLRN
