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Database: UniProt
Entry: E4QBQ4_CALH1
LinkDB: E4QBQ4_CALH1
Original site: E4QBQ4_CALH1 
ID   E4QBQ4_CALH1            Unreviewed;       175 AA.
AC   E4QBQ4;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 68.
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   OrderedLocusNames=Calhy_1554 {ECO:0000313|EMBL:ADQ07270.1};
OS   Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 / 108).
OC   Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=632292 {ECO:0000313|EMBL:ADQ07270.1, ECO:0000313|Proteomes:UP000006890};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=108;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT   "Complete sequence of Caldicellulosiruptor hydrothermalis 108.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ07270.1, ECO:0000313|Proteomes:UP000006890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18901 / VKM B-2411 / 108
RC   {ECO:0000313|Proteomes:UP000006890};
RX   PubMed=21216991; DOI=10.1128/JB.01515-10;
RA   Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA   Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA   Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA   Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT   "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT   biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT   Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT   Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL   J. Bacteriol. 193:1483-1484(2011).
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; CP002219; ADQ07270.1; -; Genomic_DNA.
DR   RefSeq; WP_013403438.1; NC_014652.1.
DR   AlphaFoldDB; E4QBQ4; -.
DR   STRING; 632292.Calhy_1554; -.
DR   KEGG; chd:Calhy_1554; -.
DR   eggNOG; COG0041; Bacteria.
DR   HOGENOM; CLU_094982_2_0_9; -.
DR   OMA; SNSIDGW; -.
DR   OrthoDB; 9791908at2; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000006890; Chromosome.
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; 3.40.50.1970; -; 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; 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|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01929};
KW   Lyase {ECO:0000313|EMBL:ADQ07270.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01929}.
FT   DOMAIN          4..153
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   175 AA;  18920 MW;  A65FF98D0C447B4F CRC64;
     MKKPLVGIIM GSDSDLPVMK EAAKVLENFG IEYEITIVSA HRTPERMFKY AKEAELRGIE
     VIIAGAGGAA HLPGMVASIS SLPVIGVPVK TSSLNGLDSL MSIVQMPAGV PVATVAINNA
     KNAGILAAQI LSIKYPQIRQ KIIEYKEKMK KEVEEKAKNL ENIGYEEYLG RKQNG
//
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