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DEOB_STRR6
ID   DEOB_STRR6              Reviewed;         403 AA.
AC   Q8DQD0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 114.
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}; OrderedLocusNames=spr0732;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15720398; DOI=10.1111/j.1742-4658.2005.04560.x;
RA   Novakova L., Saskova L., Pallova P., Janecek J., Novotna J., Ulrych A.,
RA   Echenique J., Trombe M.C., Branny P.;
RT   "Characterization of a eukaryotic type serine/threonine protein kinase and
RT   protein phosphatase of Streptococcus pneumoniae and identification of
RT   kinase substrates.";
RL   FEBS J. 272:1243-1254(2005).
CC   -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC       pentose. {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-ribose 1-phosphate = D-ribose 5-phosphate;
CC         Xref=Rhea:RHEA:18793, ChEBI:CHEBI:57720, ChEBI:CHEBI:78346;
CC         EC=5.4.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00740};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-
CC         phosphate; Xref=Rhea:RHEA:27658, ChEBI:CHEBI:57259,
CC         ChEBI:CHEBI:62877; EC=5.4.2.7; Evidence={ECO:0000255|HAMAP-
CC         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-Rule:MF_00740};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC       1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC       D-ribose 5-phosphate (route II): step 1/3. {ECO:0000255|HAMAP-
CC       Rule:MF_00740}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15720398}.
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00740}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK99536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE007317; AAK99536.1; ALT_INIT; Genomic_DNA.
DR   PIR; D97963; D97963.
DR   RefSeq; NP_358326.1; NC_003098.1.
DR   RefSeq; WP_000033108.1; NC_003098.1.
DR   AlphaFoldDB; Q8DQD0; -.
DR   SMR; Q8DQD0; -.
DR   STRING; 171101.spr0732; -.
DR   EnsemblBacteria; AAK99536; AAK99536; spr0732.
DR   GeneID; 60232573; -.
DR   KEGG; spr:spr0732; -.
DR   PATRIC; fig|171101.6.peg.811; -.
DR   eggNOG; COG1015; Bacteria.
DR   HOGENOM; CLU_053861_0_0_9; -.
DR   UniPathway; UPA00087; UER00173.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
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:UniProtKB-UniRule.
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; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR010045; DeoB.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
DR   PANTHER; PTHR21110; PTHR21110; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001491; Ppentomutase; 1.
DR   SUPFAM; SSF143856; SSF143856; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   TIGRFAMs; TIGR01696; deoB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isomerase; Manganese; Metal-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..403
FT                   /note="Phosphopentomutase"
FT                   /id="PRO_0000199853"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         303
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         340
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
FT   BINDING         351
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00740"
SQ   SEQUENCE   403 AA;  44155 MW;  0A8C5033FA4F817D CRC64;
     MSKFNRIHLV VLDSVGIGAA PDANNFVNAG VPDGASDTLG HISKTVGLNV PNMAKIGLGN
     IPRETPLKTV AAESNPTGYA TKLEEVSLGK DTMTGHWEIM GLNITEPFDT FWNGFPEEIL
     TKIEEFSGRK VIRETNKPYS GTAVIYDFGP RQMETGELII YTSADPVLQI AAHEDIIPLD
     ELYRICEYAR SITLERPALL GRIIARPYVG EPGNFTRTAN RRDLAVSPFS PTVLDKLNEA
     GIDTYAVGKI NDIFNGAGIN HDMGHNKSNS HGIDTLLKTM GLAEFEKGFS FTNLVDFDAL
     YGHRRNAHGY RDCLHEFDER LPEIIAAMRE NDLLLITADH GNDPTYAGTD HTREYIPLLA
     YSPAFKGNGL IPVGHFADIS ATVADNFGVE TAMIGESFLD KLV
 
 
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