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Database: UniProt
Entry: L7W7D9_NONDD
LinkDB: L7W7D9_NONDD
Original site: L7W7D9_NONDD 
ID   L7W7D9_NONDD            Unreviewed;       156 AA.
AC   L7W7D9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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   ECO:0000313|EMBL:AGC77605.1};
GN   OrderedLocusNames=DDD_2478 {ECO:0000313|EMBL:AGC77605.1};
OS   Nonlabens dokdonensis (strain DSM 17205 / KCTC 12402 / DSW-6) (Donghaeana
OS   dokdonensis).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=592029 {ECO:0000313|EMBL:AGC77605.1, ECO:0000313|Proteomes:UP000011173};
RN   [1] {ECO:0000313|EMBL:AGC77605.1, ECO:0000313|Proteomes:UP000011173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17205 / KCTC 12402 / DSW-6
RC   {ECO:0000313|Proteomes:UP000011173};
RX   PubMed=23292138; DOI=10.1093/gbe/evs134;
RA   Kwon S.K., Kim B.K., Song J.Y., Kwak M.J., Lee C.H., Yoon J.H., Oh T.K.,
RA   Kim J.F.;
RT   "Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana)
RT   dokdonensis DSW-6 and identification of a novel class of rhodopsins.";
RL   Genome Biol. Evol. 5:187-187(2013).
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; CP001397; AGC77605.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7W7D9; -.
DR   STRING; 592029.DDD_2478; -.
DR   KEGG; ndo:DDD_2478; -.
DR   PATRIC; fig|592029.3.peg.2456; -.
DR   eggNOG; COG0041; Bacteria.
DR   HOGENOM; CLU_094982_2_0_10; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000011173; 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:AGC77605.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01929}.
FT   DOMAIN          1..145
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         3
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         6
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   156 AA;  16205 MW;  7186457BA81F0EB3 CRC64;
     MGSTSDLPVM QDAIDVLKEL EIEIQVDVVS AHRTPEKMFE FGKTAHEKGI AVIIAGAGGA
     AHLPGMVASL SPLPVIGVPV KSSNSIDGWD SVLSILQMPG GVPVATVALN GAKNAGILAA
     QIIGATQEDV RARIISYKLG LKEKVTQAAA QMRKNV
//
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