(data stored in ACNUC7421 zone)

SWISSPROT: DEOB_EDWI9

ID   DEOB_EDWI9              Reviewed;         407 AA.
AC   C5BHJ4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 51.
DE   RecName: Full=Phosphopentomutase {ECO:0000255|HAMAP-Rule:MF_00740};
DE            EC=5.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00740};
DE   AltName: Full=Phosphodeoxyribomutase {ECO:0000255|HAMAP-Rule:MF_00740};
GN   Name=deoB {ECO:0000255|HAMAP-Rule:MF_00740};
GN   OrderedLocusNames=NT01EI_0564;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC       pentose. {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
CC       alpha-D-ribose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00740};
CC       Note=Binds 1 or 2 manganese ions. {ECO:0000255|HAMAP-
CC       Rule:MF_00740};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC       ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC       diphosphate from D-ribose 5-phosphate (route II): step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00740}.
DR   EMBL; CP001600; ACR67793.1; -; Genomic_DNA.
DR   RefSeq; WP_015869993.1; NC_012779.2.
DR   ProteinModelPortal; C5BHJ4; -.
DR   SMR; C5BHJ4; -.
DR   STRING; 634503.NT01EI_0564; -.
DR   EnsemblBacteria; ACR67793; ACR67793; NT01EI_0564.
DR   GeneID; 7960332; -.
DR   KEGG; eic:NT01EI_0564; -.
DR   PATRIC; fig|634503.3.peg.509; -.
DR   eggNOG; ENOG4105CZG; Bacteria.
DR   eggNOG; COG1015; LUCA.
DR   HOGENOM; HOG000008159; -.
DR   KO; K01839; -.
DR   OMA; CHASGTE; -.
DR   OrthoDB; POG091H00WE; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR   CDD; cd16009; PPM; 1.
DR   Gene3D; 3.30.70.1250; -; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   HAMAP; MF_00740; Phosphopentomut; 1.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR010045; DeoB.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR024052; Phosphopentomutase_DeoB_cap.
DR   PANTHER; PTHR21110; PTHR21110; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001491; Ppentomutase; 1.
DR   SUPFAM; SSF143856; SSF143856; 1.
DR   SUPFAM; SSF53649; SSF53649; 2.
DR   TIGRFAMs; TIGR01696; deoB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHJ4.
DR   SWISS-2DPAGE; C5BHJ4.
KW   Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    407       Phosphopentomutase.
FT                                /FTId=PRO_1000212808.
FT   METAL        10     10       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00740}.
FT   METAL       311    311       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00740}.
FT   METAL       347    347       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00740}.
FT   METAL       348    348       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00740}.
FT   METAL       359    359       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00740}.
SQ   SEQUENCE   407 AA;  44457 MW;  FE00BE509820B384 CRC64;
     MKRAFIMVLD SFGIGEAKDA KSFGDEGADT LGHIARACAR GEADIGRQGP LHLPNLSRLG
     LGKAALESTG RFPEGLDENA EVIGAYGYAN ELSSGKDTPS GHWEIAGVPV LFDWGYFHEH
     QNSFPQALLD TLVERANLPG YLGNCHSSGT VILDQLGEEH MKSGKPIFYT SADSVFQIAC
     HEETFGLERL YELCEIARDE LNKGGYNIGR VIARPFVGDK AGHFQRTGNR HDLAVEPPAP
     TMLKKLVDEK QGDVVSIGKI ADIYANVGIT KKVKATGIDA LFDATLQEMR QAGNDTIVFT
     NFVDFDSSYG HRRDVAGYAA ALELFDRRLP EMLALVKEDD ILILTADHGC DPTWHGSDHT
     REHIPVLVYG PKVKPGSLGE RDTFADIGQT VARYFGLSPM AYGKPMF
//

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