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Phosphopentomutase (EC 5.4.2.7) (Phosphodeoxyribomutase)
DEOB_STRA5 Reviewed; 403 AA.
Q8CMH6;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-FEB-2018, entry version 95.
RecName: Full=Phosphopentomutase {ECO:0000255|HAMAP-Rule:MF_00740};
EC=5.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00740};
AltName: Full=Phosphodeoxyribomutase {ECO:0000255|HAMAP-Rule:MF_00740};
Name=deoB1 {ECO:0000255|HAMAP-Rule:MF_00740}; Synonyms=deoB-1;
OrderedLocusNames=SAG1182;
and
Name=deoB2 {ECO:0000255|HAMAP-Rule:MF_00740}; Synonyms=deoB-2;
OrderedLocusNames=SAG2069;
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=208435;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-611 / 2603 V/R;
PubMed=12200547; DOI=10.1073/pnas.182380799;
Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
Fraser C.M.;
"Complete genome sequence and comparative genomic analysis of an
emerging human pathogen, serotype V Streptococcus agalactiae.";
Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
-!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
pentose. {ECO:0000255|HAMAP-Rule:MF_00740}.
-!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}.
-!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
alpha-D-ribose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_00740};
Note=Binds 1 or 2 manganese ions. {ECO:0000255|HAMAP-
Rule:MF_00740};
-!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
diphosphate from D-ribose 5-phosphate (route II): step 1/3.
{ECO:0000255|HAMAP-Rule:MF_00740}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00740}.
-!- SIMILARITY: Belongs to the phosphopentomutase family.
{ECO:0000255|HAMAP-Rule:MF_00740}.
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EMBL; AE009948; AAN00064.1; -; Genomic_DNA.
EMBL; AE009948; AAN00928.1; -; Genomic_DNA.
RefSeq; NP_688191.1; NC_004116.1.
RefSeq; NP_689055.1; NC_004116.1.
RefSeq; WP_000077187.1; NC_004116.1.
ProteinModelPortal; Q8CMH6; -.
SMR; Q8CMH6; -.
EnsemblBacteria; AAN00064; AAN00064; SAG1182.
EnsemblBacteria; AAN00928; AAN00928; SAG2069.
GeneID; 1013989; -.
GeneID; 1014880; -.
KEGG; sag:SAG1182; -.
KEGG; sag:SAG2069; -.
PATRIC; fig|208435.3.peg.1189; -.
HOGENOM; HOG000008159; -.
KO; K01839; -.
OMA; CHASGTE; -.
UniPathway; UPA00087; UER00173.
Proteomes; UP000000821; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-EC.
GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
CDD; cd16009; PPM; 1.
Gene3D; 3.30.70.1250; -; 1.
Gene3D; 3.40.720.10; -; 2.
HAMAP; MF_00740; Phosphopentomut; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR010045; DeoB.
InterPro; IPR006124; Metalloenzyme.
InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
PANTHER; PTHR21110; PTHR21110; 1.
Pfam; PF01676; Metalloenzyme; 1.
PIRSF; PIRSF001491; Ppentomutase; 1.
SUPFAM; SSF143856; SSF143856; 1.
SUPFAM; SSF53649; SSF53649; 2.
TIGRFAMs; TIGR01696; deoB; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding;
Reference proteome.
CHAIN 1 403 Phosphopentomutase.
/FTId=PRO_0000199850.
METAL 13 13 Manganese. {ECO:0000255|HAMAP-
Rule:MF_00740}.
METAL 303 303 Manganese. {ECO:0000255|HAMAP-
Rule:MF_00740}.
METAL 339 339 Manganese. {ECO:0000255|HAMAP-
Rule:MF_00740}.
METAL 340 340 Manganese. {ECO:0000255|HAMAP-
Rule:MF_00740}.
METAL 351 351 Manganese. {ECO:0000255|HAMAP-
Rule:MF_00740}.
SEQUENCE 403 AA; 44202 MW; 1B2D6A62D2C3ED60 CRC64;
MSQFDRIHLV VLDSVGIGAA PDANDFVNAG VPDGASDTLG HISKTVGLAV PNMAKIGLGN
IPRPQALKTV PAEENPSGYA TKLQEVSLGK DTMTGHWEIM GLNITEPFDT FWNGFPEDII
TKIEDFSGRK VIREANKPYS GTAVIDDFGP RQMETGELII YTSADPVLQI AAHEDIIPLE
ELYRICEYAR SITMERPALL GRIIARPYVG EPGNFTRTAN RHDYAVSPFE DTVLNKLDQA
GIDTYAVGKI NDIFNGSGIN HDMGHNKSNS HGIDTLIKTM GLSEFEKGFS FTNLVDFDAL
YGHRRDPHGY RDCLHEFDER LPEIISAMRD KDLLLITADH GNDPTYAGTD HTREYIPLLA
YSPSFTGNGL IPVGHFADIS ATVADNFGVD TAMIGESFLQ DLV
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EIAAB30733 | Glucose phosphomutase 2,Mouse,Mus musculus,PGM 2,Pgm2,Phosphodeoxyribomutase,Phosphoglucomutase-2,Phosphopentomutase | ||
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[PGM2] Phosphoglucomutase-2 (PGM 2) (EC 5.4.2.2) (Glucose phosphomutase 2) (Phosphodeoxyribomutase) (Phosphopentomutase) (EC 5.4.2.7)
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