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Database: UniProt
Entry: A0A136LK29_9CHLR
LinkDB: A0A136LK29_9CHLR
Original site: A0A136LK29_9CHLR 
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
//
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