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Database: UniProt
Entry: Q4J9J3_SULAC
LinkDB: Q4J9J3_SULAC
Original site: Q4J9J3_SULAC 
ID   Q4J9J3_SULAC            Unreviewed;       157 AA.
AC   Q4J9J3;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE            Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE            EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
GN   Name=purE {ECO:0000256|HAMAP-Rule:MF_01929,
GN   ECO:0000313|EMBL:AAY80537.1};
GN   OrderedLocusNames=Saci_1190 {ECO:0000313|EMBL:AAY80537.1};
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779 {ECO:0000313|EMBL:AAY80537.1, ECO:0000313|Proteomes:UP000001018};
RN   [1] {ECO:0000313|EMBL:AAY80537.1, ECO:0000313|Proteomes:UP000001018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770
RC   {ECO:0000313|Proteomes:UP000001018};
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC       (CAIR). {ECO:0000256|HAMAP-Rule:MF_01929,
CC       ECO:0000256|PIRNR:PIRNR001338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-
CC         amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate;
CC         Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}.
CC   -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01929}.
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DR   EMBL; CP000077; AAY80537.1; -; Genomic_DNA.
DR   RefSeq; WP_011278039.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4J9J3; -.
DR   STRING; 330779.Saci_1190; -.
DR   GeneID; 78441536; -.
DR   KEGG; sai:Saci_1190; -.
DR   PATRIC; fig|330779.12.peg.1154; -.
DR   eggNOG; arCOG02464; Archaea.
DR   HOGENOM; CLU_094982_2_0_2; -.
DR   OMA; SNSIDGW; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   HAMAP; MF_01929; PurE_classI; 1.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR024694; PurE_prokaryotes.
DR   NCBIfam; TIGR01162; purE; 1.
DR   PANTHER; PTHR23046:SF2; AIR CARBOXYLASE; 1.
DR   PANTHER; PTHR23046; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00731; AIRC; 1.
DR   PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01929};
KW   Lyase {ECO:0000313|EMBL:AAY80537.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01929}; Reference proteome {ECO:0000313|Proteomes:UP000001018}.
FT   DOMAIN          2..151
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   157 AA;  16903 MW;  73212AD99F441DBE CRC64;
     MPKVAVIMGS KNDWEYMKDA VDILKEFGVE VEVRVVSAHR TPEFMMEFAK TASQKGIEVI
     IAGAGGAAHL PGMTASLTHL PVIGVPVPSK NLNGLDSLLS IVQMPYGVPV ATVAIGNSKN
     AALLALRILG IKYSEIAERI KKFMEDMKSE VLNTKLP
//
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