PUR7_STRPN
ID PUR7_STRPN Reviewed; 235 AA.
AC Q07296;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase;
GN Name=purC; OrderedLocusNames=SP_0044;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rx / CP1200;
RX PubMed=8407811; DOI=10.1128/jb.175.19.6364-6367.1993;
RA Hui F.M., Morrison D.A.;
RT "Identification of a purC gene from Streptococcus pneumoniae.";
RL J. Bacteriol. 175:6364-6367(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RC STRAIN=Rx / CP1200;
RX PubMed=7883181; DOI=10.1016/0378-1119(94)00841-f;
RA Hui F.M., Zhou L., Morrison D.A.;
RT "Competence for genetic transformation in Streptococcus pneumoniae:
RT organization of a regulatory locus with homology to two lactococcin A
RT secretion genes.";
RL Gene 153:25-31(1995).
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}.
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DR EMBL; M36180; AAA69512.1; -; Genomic_DNA.
DR EMBL; L15190; AAA03540.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74233.1; -; Genomic_DNA.
DR PIR; A36941; A36941.
DR PIR; H95004; H95004.
DR RefSeq; WP_000043309.1; NZ_AKBW01000001.1.
DR PDB; 4FE2; X-ray; 2.29 A; A/B=1-235.
DR PDB; 4FGR; X-ray; 2.60 A; A/B=1-235.
DR PDB; 4NYE; X-ray; 2.69 A; A/B=1-235.
DR PDBsum; 4FE2; -.
DR PDBsum; 4FGR; -.
DR PDBsum; 4NYE; -.
DR AlphaFoldDB; Q07296; -.
DR SMR; Q07296; -.
DR STRING; 170187.SP_0044; -.
DR EnsemblBacteria; AAK74233; AAK74233; SP_0044.
DR KEGG; spn:SP_0044; -.
DR eggNOG; COG0152; Bacteria.
DR OMA; EFCYKND; -.
DR PhylomeDB; Q07296; -.
DR BRENDA; 6.3.2.6; 1960.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000000585; 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_0000100882"
FT CONFLICT 62
FT /note="V -> A (in Ref. 1; AAA69512/AAA03540)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="G -> D (in Ref. 1; AAA69512/AAA03540)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="T -> A (in Ref. 1; AAA69512/AAA03540)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 144..166
FT /evidence="ECO:0007829|PDB:4FE2"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4FE2"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4FE2"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:4FE2"
SQ SEQUENCE 235 AA; 27003 MW; C9B5601921400DD8 CRC64;
MSKQLIYSGK AKDIYTTEDE NLIISTYKDQ ATAFNGVKKE QIAGKGVLNN QISSFIFEKL
NVAGVATHFV EKLSDTEQLN KKVKIIPLEV VLRNYTAGSF SKRFGVDEGI ALETPIVEFY
YKNDDLDDPF INDEHVKFLQ IAGDQQIAYL KEETRRINEL LKVWFAEIGL KLIDFKLEFG
FDKDGKIILA DEFSPDNCRL WDADGNHMDK DVFRRGLGEL TDVYEIVWEK LQELK
