PURE_HAEIN
ID PURE_HAEIN Reviewed; 164 AA.
AC P43849;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
DE Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929};
DE EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
GN Name=purE {ECO:0000255|HAMAP-Rule:MF_01929}; OrderedLocusNames=HI_1615;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
RC STRAIN=AM30 (770235) / Serotype B;
RX PubMed=7997179; DOI=10.1111/j.1365-2958.1994.tb00461.x;
RA van Ham M.S., van Alphen L., Mooi F.R., van Putten J.P.M.;
RT "The fimbrial gene cluster of Haemophilus influenzae type b.";
RL Mol. Microbiol. 13:673-684(1994).
CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929}.
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:0000255|HAMAP-
CC Rule:MF_01929};
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:0000255|HAMAP-Rule:MF_01929}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01929}.
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DR EMBL; L42023; AAC23263.1; -; Genomic_DNA.
DR EMBL; Z33502; CAA83909.1; -; Genomic_DNA.
DR PIR; G64132; G64132.
DR PIR; S54434; S54434.
DR RefSeq; NP_439757.1; NC_000907.1.
DR RefSeq; WP_005693627.1; NC_000907.1.
DR AlphaFoldDB; P43849; -.
DR SMR; P43849; -.
DR STRING; 71421.HI_1615; -.
DR EnsemblBacteria; AAC23263; AAC23263; HI_1615.
DR KEGG; hin:HI_1615; -.
DR PATRIC; fig|71421.8.peg.1688; -.
DR eggNOG; COG0041; Bacteria.
DR HOGENOM; CLU_094982_2_2_6; -.
DR OMA; SNSIDGW; -.
DR PhylomeDB; P43849; -.
DR BioCyc; HINF71421:G1GJ1-1628-MON; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000000579; 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 HAMAP; MF_01929; PurE_classI; 1.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR Pfam; PF00731; AIRC; 1.
DR PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
DR TIGRFAMs; TIGR01162; purE; 1.
PE 3: Inferred from homology;
KW Isomerase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..164
FT /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT /id="PRO_0000074975"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT CONFLICT 139..143
FT /note="DALFT -> AELLS (in Ref. 2; CAA83909)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="A -> S (in Ref. 2; CAA83909)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="N -> S (in Ref. 2; CAA83909)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="NM -> RA (in Ref. 2; CAA83909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 17269 MW; 60A03B0D4DD85412 CRC64;
MSKTAQIAVV MGSKSDWATM QEATQILDEL NVPYHVEVVS AHRTPDKLFE FAENAQKNGY
KVIIAGAGGA AHLPGMIAAK TLVPVLGVPV KSSMLSGVDS LYSIVQMPKG IPVGTLAIGP
AGAANAGLLA AQILAGWDDA LFTRLQAFRE NQTNMVLDNP DPRT