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Database: UniProt
Entry: F2LVE5_HIPMA
LinkDB: F2LVE5_HIPMA
Original site: F2LVE5_HIPMA 
ID   F2LVE5_HIPMA            Unreviewed;       156 AA.
AC   F2LVE5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-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=Hipma_0759 {ECO:0000313|EMBL:AEA33729.1};
OS   Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2).
OC   Bacteria; Campylobacterota; Desulfurellia; Desulfurellales; Hippeaceae;
OC   Hippea.
OX   NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA33729.1, ECO:0000313|Proteomes:UP000008139};
RN   [1] {ECO:0000313|EMBL:AEA33729.1, ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RX   PubMed=21886857;
RA   Huntemann M., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Rohde M., Spring S., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Mavromatis K.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer Hippea
RT   maritima type strain (MH(2)).";
RL   Stand. Genomic Sci. 4:303-311(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Hippea maritima DSM 10411.";
RL   Submitted (MAR-2011) 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; CP002606; AEA33729.1; -; Genomic_DNA.
DR   RefSeq; WP_013681770.1; NC_015318.1.
DR   AlphaFoldDB; F2LVE5; -.
DR   STRING; 760142.Hipma_0759; -.
DR   KEGG; hmr:Hipma_0759; -.
DR   eggNOG; COG0041; Bacteria.
DR   HOGENOM; CLU_094982_2_2_7; -.
DR   InParanoid; F2LVE5; -.
DR   OrthoDB; 9791908at2; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000008139; 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; 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   Lyase {ECO:0000313|EMBL:AEA33729.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01929}; Reference proteome {ECO:0000313|Proteomes:UP000008139}.
FT   DOMAIN          1..150
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   156 AA;  16741 MW;  FED2961CD9D010C8 CRC64;
     MKVAIVAGSK SDEEIMNAAR EVLDEFGVTH KEFIASAHRS PNLTKEVAQI IEDEFDVAIV
     IAGLSAALPG VIAAYTNKPV LGVPVASDLM GLDALFSIAQ MPRGIPVATF GIGKKGAKNA
     ALFAIRILSL KNPTLLERLK DKARSEEEEL RKLNDM
//
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