PUR7_THEMA
ID PUR7_THEMA Reviewed; 230 AA.
AC Q9X0X0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase;
GN Name=purC; OrderedLocusNames=TM_1243;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36318.1; -; Genomic_DNA.
DR PIR; E72276; E72276.
DR RefSeq; NP_229048.1; NC_000853.1.
DR RefSeq; WP_004080029.1; NZ_CP011107.1.
DR PDB; 1KUT; X-ray; 2.20 A; A/B=1-230.
DR PDBsum; 1KUT; -.
DR AlphaFoldDB; Q9X0X0; -.
DR SMR; Q9X0X0; -.
DR STRING; 243274.THEMA_08120; -.
DR EnsemblBacteria; AAD36318; AAD36318; TM_1243.
DR KEGG; tma:TM1243; -.
DR eggNOG; COG0152; Bacteria.
DR InParanoid; Q9X0X0; -.
DR OMA; EFCYKND; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR EvolutionaryTrace; Q9X0X0; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
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; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..230
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_0000100891"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 39..56
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1KUT"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 138..160
FT /evidence="ECO:0007829|PDB:1KUT"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1KUT"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1KUT"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1KUT"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:1KUT"
SQ SEQUENCE 230 AA; 26231 MW; 242B18AD026DB4A9 CRC64;
MNYEGKTKIV KVTGDYALLE FKDDITAGDG LKHDVLTGKG SICAETTAIL MKYLSEKGIK
THLVEYIPPR TLKVIPLKMF PLEVVVRLKK AGSFVRRYGG AEGEDLPVPL VEFFIKDDER
HDPMVCVDHL EILGIATKKQ AEKMKEAAVK ITLALKEFFE RANFELWDIK YEFGLDKDGN
VVLGDEISPD TFRLRKKGEI FDKDVYRRDL GDPLKKYREV LELCRSLNSQ
