ID D8GI16_CLOLD Unreviewed; 393 AA.
AC D8GI16;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 18.
DE RecName: Full=Phosphopentomutase;
DE EC=5.4.2.7;
DE AltName: Full=Phosphodeoxyribomutase;
GN Name=deoB; OrderedLocusNames=CLJU_c18150;
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC;
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform
RT based on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
CC -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC pentose (By similarity).
CC -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
CC alpha-D-ribose 5-phosphate.
CC -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
CC phosphate.
CC -!- COFACTOR: Binds 1 or 2 manganese ions (By similarity).
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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phosphopentomutase family.
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DR EMBL; CP001666; ADK14878.1; -; Genomic_DNA.
DR RefSeq; YP_003779980.1; NC_014328.1.
DR EnsemblBacteria; ADK14878; ADK14878; CLJU_c18150.
DR GeneID; 9445432; -.
DR KEGG; clj:CLJU_c18150; -.
DR PATRIC; 42484865; VBICloLju82977_1799.
DR HOGENOM; HOG000008159; -.
DR KO; K01839; -.
DR BioCyc; CLJU748727:GHMO-1815-MONOMER; -.
DR UniPathway; UPA00087; UER00173.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:HAMAP.
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:0009264; P:deoxyribonucleotide catabolic process; IEA:HAMAP.
DR Gene3D; 3.30.70.1250; -; 1.
DR Gene3D; 3.40.720.10; -; 2.
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 Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001491; Ppentomutase; 1.
DR SUPFAM; SSF53649; Alkaline_phosphatase_core; 1.
DR SUPFAM; SSF143856; SSF143856; 1.
DR TIGRFAMs; TIGR01696; deoB; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding.
FT METAL 13 13 Manganese (By similarity).
FT METAL 292 292 Manganese (By similarity).
FT METAL 328 328 Manganese (By similarity).
FT METAL 329 329 Manganese (By similarity).
FT METAL 340 340 Manganese (By similarity).
SQ SEQUENCE 393 AA; 44362 MW; 3015796BE92DA364 CRC64;
MNEFKRIHVI VMDSVGIGEA PDSEKFGDVG VNTLAHIAEK KNGLNIPNME AMGLSNIYEI
KGVKRAAHPK AYFTKMQESS RGKDTMTGHW EMMGLYIDKP FRVFPNGFPD ELIKKIEDFS
GRKVIANKPA SGTEIIKELG ERQLKTGELI VYTSADSVLQ IAAHEEVIPL DELYKICQYC
RDITLDEPYK LGRIIARPYV GKTADTFKRT SNRHDYALKP FGETVMDYIK NAGLDSIAIG
KIRDIFDGEG VTKAIRTKSN MDGMDKFISV LDEDFHGLSF TNLVDFDAVY GHRRNPIGYG
DAIEAFDKRL TEVFEKLRED DLLIVTADHG NDPTYTGTDH TREFVPLLVY SKRFEEGKDL
GIRRTFSDIG ATIADNFKVK MPKYGESFLQ KLI
//
