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Database: UniProt
Entry: A0A0P7GPM2_9EURY
LinkDB: A0A0P7GPM2_9EURY
Original site: A0A0P7GPM2_9EURY 
ID   A0A0P7GPM2_9EURY        Unreviewed;       195 AA.
AC   A0A0P7GPM2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE            Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE            EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
GN   Name=purE {ECO:0000256|HAMAP-Rule:MF_01929,
GN   ECO:0000313|EMBL:KPN30986.1};
GN   ORFNames=SY89_01728 {ECO:0000313|EMBL:KPN30986.1};
OS   Halolamina pelagica.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae.
OX   NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN30986.1, ECO:0000313|Proteomes:UP000050535};
RN   [1] {ECO:0000313|Proteomes:UP000050535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA   Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA   Schwartz K.J., Yoon K.;
RL   Submitted (NOV-2013) 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|HAMAP-Rule:MF_01929}.
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};
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}.
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:KPN30986.1}.
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DR   EMBL; LGUC01000001; KPN30986.1; -; Genomic_DNA.
DR   RefSeq; WP_054583758.1; NZ_LGUC01000001.1.
DR   AlphaFoldDB; A0A0P7GPM2; -.
DR   STRING; 699431.SY89_01728; -.
DR   PATRIC; fig|699431.3.peg.1768; -.
DR   OrthoDB; 9473at2157; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000050535; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000050535}.
FT   DOMAIN          25..184
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   REGION          176..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
SQ   SEQUENCE   195 AA;  20357 MW;  F1A95FB1160EEF29 CRC64;
     MPAVTDLIDR LESDAAADRP AEATPDVGII MGSDSDLDTM QGAFDALDAL GFAEQTDHAH
     PPEGQFSYES YVVSAHRTPD LMYAYAETAA DRGLDVIVAG AGGKSADLPN MTASIAFPLP
     VIGVPVQEKS VDSVIGMPTG APITAVDAGK SYNAALSAAQ ILAREHPTVR DRLEELHADR
     REGVGDVSSS LHDLG
//
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