PUR7_PYRHO
ID PUR7_PYRHO Reviewed; 238 AA.
AC O57978;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase;
GN Name=purC; OrderedLocusNames=PH0239;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29311.1; -; Genomic_DNA.
DR PIR; H71247; H71247.
DR PDB; 3U54; X-ray; 2.35 A; A/B=1-238.
DR PDB; 3U55; X-ray; 1.90 A; A=1-238.
DR PDB; 4O7L; X-ray; 2.10 A; A=1-238.
DR PDB; 4O7N; X-ray; 2.16 A; A=1-238.
DR PDB; 4O7R; X-ray; 2.35 A; A=1-238.
DR PDB; 4O7S; X-ray; 2.24 A; A=1-238.
DR PDB; 4O7T; X-ray; 2.10 A; A=1-238.
DR PDB; 4O7V; X-ray; 2.30 A; A=1-238.
DR PDB; 4O7W; X-ray; 2.20 A; A=1-238.
DR PDB; 4O7Y; X-ray; 2.00 A; A=1-238.
DR PDB; 4O7Z; X-ray; 2.30 A; A=1-238.
DR PDB; 4O81; X-ray; 2.10 A; A/B=1-238.
DR PDB; 4O82; X-ray; 2.16 A; A/B=1-238.
DR PDB; 4O83; X-ray; 2.05 A; A/B=1-238.
DR PDB; 4O84; X-ray; 2.09 A; A/B=1-238.
DR PDB; 4O86; X-ray; 2.20 A; A=1-238.
DR PDBsum; 3U54; -.
DR PDBsum; 3U55; -.
DR PDBsum; 4O7L; -.
DR PDBsum; 4O7N; -.
DR PDBsum; 4O7R; -.
DR PDBsum; 4O7S; -.
DR PDBsum; 4O7T; -.
DR PDBsum; 4O7V; -.
DR PDBsum; 4O7W; -.
DR PDBsum; 4O7Y; -.
DR PDBsum; 4O7Z; -.
DR PDBsum; 4O81; -.
DR PDBsum; 4O82; -.
DR PDBsum; 4O83; -.
DR PDBsum; 4O84; -.
DR PDBsum; 4O86; -.
DR AlphaFoldDB; O57978; -.
DR SMR; O57978; -.
DR STRING; 70601.3256628; -.
DR EnsemblBacteria; BAA29311; BAA29311; BAA29311.
DR KEGG; pho:PH0239; -.
DR eggNOG; arCOG04421; Archaea.
DR OMA; EFCYKND; -.
DR BRENDA; 6.3.2.6; 5244.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000000752; 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..238
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_0000100916"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3U55"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3U55"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3U55"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:3U55"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:3U55"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:3U55"
FT HELIX 143..165
FT /evidence="ECO:0007829|PDB:3U55"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3U55"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3U55"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3U55"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3U55"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:3U55"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:3U55"
SQ SEQUENCE 238 AA; 27436 MW; 2C161C59792486E7 CRC64;
MVKLMEVYEG KAKKMIPIDD DKLIMEFKDD ATAFDGTKKA RFKGKGWLNA QLSVIFFKLL
EEHGIKTHFI GVAGGNRLIV EKLDMYPLEV VVRNVVAGSL KKRLPLPEGY ELPEPIVELY
YKNDELHDPM INYYHAKVLG ISLDEIKKIE EIALKVNEIL KDYLAKKGII LVDFKLEFGK
DKNGDIVLAD EISPDTCRFW DAKTKRSLDK DVFRFDKGDL IEAYKEIYER ITGEKPEF
