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Database: UniProt
Entry: K9T1U0_9CYAN
LinkDB: K9T1U0_9CYAN
Original site: K9T1U0_9CYAN 
ID   K9T1U0_9CYAN            Unreviewed;       173 AA.
AC   K9T1U0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=Ple7327_0696 {ECO:0000313|EMBL:AFY76126.1};
OS   Pleurocapsa sp. PCC 7327.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC   Pleurocapsa.
OX   NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY76126.1, ECO:0000313|Proteomes:UP000010382};
RN   [1] {ECO:0000313|EMBL:AFY76126.1, ECO:0000313|Proteomes:UP000010382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY76126.1,
RC   ECO:0000313|Proteomes:UP000010382};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished genome of Pleurocapsa sp. PCC 7327.";
RL   Submitted (MAY-2012) 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       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}.
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DR   EMBL; CP003590; AFY76126.1; -; Genomic_DNA.
DR   RefSeq; WP_015142434.1; NC_019689.1.
DR   AlphaFoldDB; K9T1U0; -.
DR   STRING; 118163.Ple7327_0696; -.
DR   KEGG; plp:Ple7327_0696; -.
DR   PATRIC; fig|118163.3.peg.771; -.
DR   eggNOG; COG0041; Bacteria.
DR   HOGENOM; CLU_094982_2_0_3; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000010382; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000010382}.
FT   DOMAIN          5..154
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   173 AA;  18431 MW;  F854401AB2A7739A CRC64;
     MSNPPLVGII MGSDSDLPTM RDAIAVCEEF GIACEVAIVS AHRTPERMVN YAQTAHQRGI
     KVIIAGAGGA AHLPGMVASL TPLPVIGVPV SSRHLQGLDS LYSIVQMPAG IPVATVAIGN
     AKNSGLLAVQ ILASHNPELL EKVRQYRQNL AQSVLEKQAK LEQLGYKQYL EQM
//
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