ID A0A136LK29_9CHLR Unreviewed; 184 AA.
AC A0A136LK29;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 Name=purE {ECO:0000313|EMBL:KXK21962.1};
GN ORFNames=UZ15_CFX003001186 {ECO:0000313|EMBL:KXK21962.1};
OS Chloroflexi bacterium OLB15.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK21962.1, ECO:0000313|Proteomes:UP000070332};
RN [1] {ECO:0000313|EMBL:KXK21962.1, ECO:0000313|Proteomes:UP000070332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB15 {ECO:0000313|EMBL:KXK21962.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK21962.1}.
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DR EMBL; LMZS01000060; KXK21962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136LK29; -.
DR STRING; 1617416.UZ15_CFX003001186; -.
DR PATRIC; fig|1617416.3.peg.1241; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000070332; 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 6..153
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT REGION 157..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001338-1"
SQ SEQUENCE 184 AA; 19433 MW; 45C65847E7D4FDF6 CRC64;
MTLLNPLVPI IMGSKSDLHY GQVIANSLNQ FGISSEIRIA SAHKVPSILL QILTDYETDP
RPKVYITVAG RSNALSGIVD AQVTCPVIAC PPLSDTFNGA DIYSSLRMPG GVAPLVILDP
EGAALAAAKI FALDNPEVNA AVRAFQKAGV DRLLQDDAEL NSKSKPSAPS QPPPQDSSVN
NFDL
//