PUR7_NITMS
ID PUR7_NITMS Reviewed; 274 AA.
AC A9A5G9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=Nmar_0784;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX12680.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A5G9; -.
DR SMR; A9A5G9; -.
DR STRING; 436308.Nmar_0784; -.
DR EnsemblBacteria; ABX12680; ABX12680; Nmar_0784.
DR KEGG; nmr:Nmar_0784; -.
DR eggNOG; arCOG04421; Archaea.
DR HOGENOM; CLU_045637_0_1_2; -.
DR OMA; TKFEFGF; -.
DR PhylomeDB; A9A5G9; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000000792; Chromosome.
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 HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
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 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..274
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000095997"
SQ SEQUENCE 274 AA; 31706 MW; 17802D1514235973 CRC64;
MEFLTSGKVK DLYDVDESTL LFKFSDRVSA YDVKFKQDIP RKGEVLCKFA EFWFNELDVP
NHFIKRESEN EILVKKMKML PIECVVRGYF YGSLVSRWKK GEVQVPEGTN TTLAAQLPEP
IFDPTTKSEH DIPIDKNKAI EMNLVSEEQY NWLEKTSIEI YKKMAKITDD VGFILADLKL
EFGILDDQIT LGDSIGPDEY RLWPKDSFEV GKIQEAYDKQ LLRDWLTANG YQKQFDDARD
NGQEPIPPNI PSEIISKMTE RYVTAYEKIS GKSL