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PURE_BRUME
ID   PURE_BRUME              Reviewed;         162 AA.
AC   P52558;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 125.
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=BMEI0296;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RA   Warren R., Hoover D., Hadfield T., Drazek S.;
RT   "Molecular cloning and genetic characterization of the purEK operon of
RT   Brucella melitensis strain 16M.";
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL51477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U10241; AAA57002.1; -; Unassigned_DNA.
DR   EMBL; AE008917; AAL51477.1; ALT_INIT; Genomic_DNA.
DR   PIR; AB3289; AB3289.
DR   RefSeq; WP_002964830.1; NZ_GG703781.1.
DR   AlphaFoldDB; P52558; -.
DR   SMR; P52558; -.
DR   STRING; 224914.BMEI0296; -.
DR   EnsemblBacteria; AAL51477; AAL51477; BMEI0296.
DR   GeneID; 45125041; -.
DR   KEGG; bme:BMEI0296; -.
DR   PATRIC; fig|224914.52.peg.1201; -.
DR   eggNOG; COG0041; Bacteria.
DR   OMA; SNSIDGW; -.
DR   PhylomeDB; P52558; -.
DR   UniPathway; UPA00074; UER00943.
DR   PRO; PR:P52558; -.
DR   Proteomes; UP000000419; Chromosome I.
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.
FT   CHAIN           1..162
FT                   /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT                   /id="PRO_0000074970"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT   CONFLICT        55
FT                   /note="A -> R (in Ref. 1; AAA57002)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67..68
FT                   /note="GA -> R (in Ref. 1; AAA57002)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   162 AA;  16596 MW;  0B812230C4EE9EE7 CRC64;
     MSVDVAIIMG SQSDWETMHH AADTLEALGI SFDARIVSAH RTPDRLVAFA KGAKAEGFKV
     IIAGAGGAAH LPGMAAAMTP LPVFGVPVQS KALSGQDSLL SIVQMPAGIP VGTLAIGRAG
     AVNAALLAAA VLALYDEALA ARLDEWRKAQ TESVAERPSN EA
 
 
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