ID   B7A6L6_THEAQ            Unreviewed;       164 AA.
AC   B7A6L6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 48.
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=TaqDRAFT_4465 {ECO:0000313|EMBL:EED10905.1};
OS   Thermus aquaticus Y51MC23.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=498848 {ECO:0000313|EMBL:EED10905.1, ECO:0000313|Proteomes:UP000005403};
RN   [1] {ECO:0000313|EMBL:EED10905.1, ECO:0000313|Proteomes:UP000005403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51MC23 {ECO:0000313|EMBL:EED10905.1,
RC   ECO:0000313|Proteomes:UP000005403};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L.,
RA   Hauser L., Saunders E., Tapia R., Green L., Rogers Y., Detter J.C.,
RA   Brettin T.S., Mead D.;
RT   "Sequencing of the draft genome and assembly of Thermus aquaticus
RT   Y51MC23.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole
CC       ribonucleotide (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(+) =
CC         5-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;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-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
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01929}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EED10905.1}.
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DR   EMBL; ABVK02000002; EED10905.1; -; Genomic_DNA.
DR   RefSeq; WP_003045057.1; NZ_CP010822.1.
DR   STRING; 498848.TaqDRAFT_4465; -.
DR   EnsemblBacteria; EED10905; EED10905; TaqDRAFT_4465.
DR   eggNOG; ENOG4108UM6; Bacteria.
DR   eggNOG; COG0041; LUCA.
DR   OrthoDB; POG091H01UJ; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000005403; Unassembled WGS sequence.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.7700; -; 1.
DR   HAMAP; MF_01929; PurE_classI; 1.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR024694; PurE_prokaryotes.
DR   InterPro; IPR035893; PurE_sf.
DR   Pfam; PF00731; AIRC; 1.
DR   PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SUPFAM; SSF52255; SSF52255; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005403};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338}; Lyase {ECO:0000313|EMBL:EED10905.1};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338}.
FT   DOMAIN        3    154       AIRC. {ECO:0000259|SMART:SM01001}.
FT   BINDING      11     11       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      14     14       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      41     41       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
SQ   SEQUENCE   164 AA;  17064 MW;  1DCB892FA7E33D77 CRC64;
     MRPLVGVIMG SRSDWATMRH AAETLEALGV PYEVRVVSAH RTPDLMAEYA KTAEARGLMV
     IIAGAGGAAH LPGMTAAHTP LPVLGVPVES QALKGLDSLL SIVQMPAGVP VGTLAIGKAG
     AVNAALLAAS IVGLRHPEVM ERVKAYRRAQ TEAVLAHPDP REEA
//