GenomeNet

Database: UniProt/TrEMBL
Entry: A2BZZ5_PROM1
LinkDB: A2BZZ5_PROM1
Original site: A2BZZ5_PROM1 
ID   A2BZZ5_PROM1            Unreviewed;       178 AA.
AC   A2BZZ5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   01-MAY-2013, entry version 45.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase;
DE            Short=N5-CAIR mutase;
DE            EC=5.4.99.18;
GN   Name=purE; OrderedLocusNames=NATL1_02411;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:E231-E231(2007).
CC   -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole
CC       ribonucleotide (CAIR) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D-
CC       ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
CC       carboxylate.
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   -!- SIMILARITY: Belongs to the AIR carboxylase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000553; ABM74805.1; -; Genomic_DNA.
DR   RefSeq; YP_001014070.1; NC_008819.1.
DR   ProteinModelPortal; A2BZZ5; -.
DR   SMR; A2BZZ5; 11-159.
DR   STRING; 167555.NATL1_02411; -.
DR   EnsemblBacteria; ABM74805; ABM74805; NATL1_02411.
DR   GeneID; 4779595; -.
DR   KEGG; pme:NATL1_02411; -.
DR   PATRIC; 23018007; VBIProMar31285_0249.
DR   eggNOG; COG0041; -.
DR   HOGENOM; HOG000034141; -.
DR   KO; K01588; -.
DR   OMA; QSDWATM; -.
DR   ProtClustDB; CLSK716096; -.
DR   BioCyc; PMAR167555:GI3K-286-MONOMER; -.
DR   UniPathway; UPA00074; UER00943.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.7700; -; 1.
DR   InterPro; IPR024694; N5-CAIR_mutase_PurE.
DR   InterPro; IPR000031; N5-CAIR_Mutase_PurE_dom.
DR   Pfam; PF00731; AIRC; 1.
DR   PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SUPFAM; SSF52255; AIR_carboxyl; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Lyase; Purine biosynthesis.
FT   BINDING      18     18       Substrate (By similarity).
FT   BINDING      21     21       Substrate (By similarity).
FT   BINDING      48     48       Substrate (By similarity).
SQ   SEQUENCE   178 AA;  18820 MW;  40BDBB919CC87D4F CRC64;
     MSLTEANTFK QVAVVMGSDS DLKTLKPAVA ILDQFGISNE VRILSAHRTP KEMMDFAQMA
     ESNGFGVIIA GAGGAAHLPG MIASLTTLPV IGVPVKSKAL SGIDSMYSIL QMPSGIPVAT
     VAIEGGLNAG LLATQILAIN NTELKNKLNA YRCELHDLVV KKDHTLKEIG AITYLEKM
//
DBGET integrated database retrieval system