ID A0A7J4KY44_9EURY Unreviewed; 164 AA. AC A0A7J4KY44; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 22-FEB-2023, entry version 6. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|PIRNR:PIRNR001338}; DE Short=N5-CAIR mutase {ECO:0000256|PIRNR:PIRNR001338}; DE EC=5.4.99.18 {ECO:0000256|PIRNR:PIRNR001338}; GN ORFNames=HA232_00590 {ECO:0000313|EMBL:HIH36394.1}; OS Methanocellales archaeon. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanocellales. OX NCBI_TaxID=2666334 {ECO:0000313|EMBL:HIH36394.1, ECO:0000313|Proteomes:UP000536663}; RN [1] {ECO:0000313|Proteomes:UP000536663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX DOI=10.1101/2020.03.01.972265; RA Rinke C., Chuvochina M., Mussig A.J., Chaumeil P.-A., Waite D.W., RA Whitman W.B., Parks D.H., Hugenholtz P.; RT "A rank-normalized archaeal taxonomy based on genome phylogeny resolves RT widespread incomplete and uneven classifications."; RL bioRxiv 0:0-0(2020). CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide CC (CAIR). {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; CC Evidence={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|PIRNR:PIRNR001338}. CC -!- SIMILARITY: Belongs to the AIR carboxylase family. CC {ECO:0000256|PIRNR:PIRNR001338}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HIH36394.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DUGN01000022; HIH36394.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7J4KY44; -. DR UniPathway; UPA00074; UER00943. DR Proteomes; UP000536663; Unassembled WGS sequence. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-EC. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.1970; -; 1. DR InterPro; IPR000031; PurE_dom. DR InterPro; IPR024694; PurE_prokaryotes. 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|PIRNR:PIRNR001338}; KW Purine biosynthesis {ECO:0000256|PIRNR:PIRNR001338}. FT DOMAIN 3..149 FT /note="PurE" FT /evidence="ECO:0000259|SMART:SM01001" FT BINDING 11 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001338-1" FT BINDING 14 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001338-1" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001338-1" SQ SEQUENCE 164 AA; 17848 MW; 0B7BAE464488D7E8 CRC64; MKDMVIILMG SNKDLNFSSS IGRTLDNLGV KYEFRAASAH KTPRKVLDIL EEYDKLERVV YITVAGRSNA LSGLVDANTT KPVIACPLYS EKFGGADIYS SLRVPSGIGS LVNIEPEGAA IAAAKILAIG NKGLTEKIQE YQMKKREEIN AADDTLKDDL NRGQ //