(data stored in ACNUC7421 zone)

SWISSPROT: E3J4W6_FRAIE

ID   E3J4W6_FRAIE            Unreviewed;       170 AA.
AC   E3J4W6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   16-JAN-2019, entry version 54.
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=FraEuI1c_0197 {ECO:0000313|EMBL:ADP78285.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78285.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78285.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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}.
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DR   EMBL; CP002299; ADP78285.1; -; Genomic_DNA.
DR   RefSeq; WP_013421408.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0197; -.
DR   EnsemblBacteria; ADP78285; ADP78285; FraEuI1c_0197.
DR   KEGG; fri:FraEuI1c_0197; -.
DR   eggNOG; ENOG4108UM6; Bacteria.
DR   eggNOG; COG0041; LUCA.
DR   HOGENOM; HOG000034141; -.
DR   KO; K01588; -.
DR   OMA; SNSIDGW; -.
DR   OrthoDB; 1701464at2; -.
DR   BioCyc; FSP298654:G1GOT-200-MONOMER; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000002484; 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; 3.40.50.7700; -; 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;
DR   PRODOM; E3J4W6.
DR   SWISS-2DPAGE; E3J4W6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338}; Lyase {ECO:0000313|EMBL:ADP78285.1};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   DOMAIN       10    159       AIRC. {ECO:0000259|SMART:SM01001}.
FT   BINDING      18     18       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      21     21       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      48     48       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
SQ   SEQUENCE   170 AA;  16735 MW;  B8E846CD89F47478 CRC64;
     MSPTSTPSRP KVAVVYGSAS DAATMSKAGA TLGRFGVEFE EAVLSAHRAP RTLADWVDGL
     RDRGVAVVIA GAGLAAALPG TVAALTTLPV IGVPISGGAL DGMDSLLAIA QMPPGVAVAT
     VGLNNATNAA VLAVQILAVS DPDLAAKLAT YKDDFEKAAA DGLARAGASA
//

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