ID A0A0S7WRJ1_9CHLR Unreviewed; 154 AA.
AC A0A0S7WRJ1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=AMJ37_02255 {ECO:0000313|EMBL:KPJ52813.1};
OS Dehalococcoidia bacterium DG_18.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703392 {ECO:0000313|EMBL:KPJ52813.1, ECO:0000313|Proteomes:UP000053383};
RN [1] {ECO:0000313|EMBL:KPJ52813.1, ECO:0000313|Proteomes:UP000053383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC_18 {ECO:0000313|EMBL:KPJ52813.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPJ52813.1}.
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DR EMBL; LIZO01000050; KPJ52813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7WRJ1; -.
DR PATRIC; fig|1703392.3.peg.433; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000053383; Unassembled WGS sequence.
DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase 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_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; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01929};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01929}.
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 154 AA; 16480 MW; EE2F699A651324B0 CRC64;
MSLVGVVMGS KSDEQLMQPA LDMLRQLGIE YEVSVISAHR NPEKTREYGL KAERRGLEVI
IAGAGKAAHL PGVLASWTTL PIIGVPLATS ELMGVDALYS MAEMPAGVPV ACVAIDGAKN
AAILAAAILA LKHEKIKVAY EEYRRSLLDS QREP
//
