ID D3S2H0_FERPA Unreviewed; 157 AA.
AC D3S2H0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000256|HAMAP-Rule:MF_02045};
DE EC=4.1.1.21 {ECO:0000256|HAMAP-Rule:MF_02045};
DE AltName: Full=AIR carboxylase {ECO:0000256|HAMAP-Rule:MF_02045};
DE Short=AIRC {ECO:0000256|HAMAP-Rule:MF_02045};
GN Name=purE {ECO:0000256|HAMAP-Rule:MF_02045};
GN OrderedLocusNames=Ferp_0320 {ECO:0000313|EMBL:ADC64500.1};
OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Ferroglobus.
OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC64500.1, ECO:0000313|Proteomes:UP000002613};
RN [1] {ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT "Complete sequence of Ferroglobus placidus DSM 10642.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC64500.1, ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX PubMed=22180810; DOI=10.4056/sigs.2225018;
RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA Lovley D., Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL Stand. Genomic Sci. 5:50-60(2011).
CC -!- FUNCTION: Catalyzes the reversible conversion of 5-aminoimidazole
CC ribonucleotide (AIR) and CO(2) to 4-carboxy-5-aminoimidazole
CC ribonucleotide (CAIR). {ECO:0000256|HAMAP-Rule:MF_02045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+)
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02045};
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 (carboxylase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004747, ECO:0000256|HAMAP-Rule:MF_02045}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class II subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02045}.
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DR EMBL; CP001899; ADC64500.1; -; Genomic_DNA.
DR RefSeq; WP_012964847.1; NC_013849.1.
DR AlphaFoldDB; D3S2H0; -.
DR STRING; 589924.Ferp_0320; -.
DR PaxDb; 589924-Ferp_0320; -.
DR GeneID; 8777818; -.
DR KEGG; fpl:Ferp_0320; -.
DR eggNOG; arCOG02464; Archaea.
DR HOGENOM; CLU_094982_2_0_2; -.
DR OrthoDB; 9473at2157; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000002613; Chromosome.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1970; -; 1.
DR HAMAP; MF_02045; PurE_classII; 1.
DR InterPro; IPR033626; PurE_classII.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR PANTHER; PTHR23046:SF2; PHOSPHORIBOSYLAMINOIMIDAZOLE 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 Lyase {ECO:0000256|HAMAP-Rule:MF_02045, ECO:0000313|EMBL:ADC64500.1};
KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02045};
KW Reference proteome {ECO:0000313|Proteomes:UP000002613}.
FT DOMAIN 1..145
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02045,
FT ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02045,
FT ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02045"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02045,
FT ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02045"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02045"
SQ SEQUENCE 157 AA; 17237 MW; 01B243F85414B86E CRC64;
MKVVIILGSK SDLEIGEKIR SKLKENFGID SEIRIASAHK TPEKVLEIIK SYEKAVFVTV
AGRSNALSGF VDANTLNPVI ASPPISDKFA GMDILSSINM PSGVAPMLVL YEENAALAVA
KIVALFDDNV RRKVEEYQRK KKEEIEKADE VVRYGNG
//
