PPM_THEKO
ID PPM_THEKO Reviewed; 450 AA.
AC Q6I7B6; Q5JJ52;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphopentomutase {ECO:0000303|PubMed:15205420};
DE Short=PPM {ECO:0000303|PubMed:15205420};
DE EC=5.4.2.7 {ECO:0000269|PubMed:15205420};
GN OrderedLocusNames=TK1777 {ECO:0000312|EMBL:BAD85966.1};
GN ORFNames=Tko0866 {ECO:0000312|EMBL:BAD23919.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 1-7,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15205420; DOI=10.1128/jb.186.13.4185-4191.2004;
RA Rashid N., Imanaka H., Fukui T., Atomi H., Imanaka T.;
RT "Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate
RT aldolase reveals a metabolic link between pentoses and central carbon
RT metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis.";
RL J. Bacteriol. 186:4185-4191(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Catalyzes the conversion of deoxyribose 1-phosphate to
CC deoxyribose 5-phosphate. Shows also weak activity with glucose 1-
CC phosphate and mannose 1-phosphate. Could be involved in pentose
CC biosynthesis. {ECO:0000269|PubMed:15205420}.
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:0000305};
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;
CC Evidence={ECO:0000269|PubMed:15205420};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15205420};
CC Note=Can also use Ni(2+), Mn(2+) and Zn(2+), to a lower extent.
CC {ECO:0000269|PubMed:15205420};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for 2-deoxy-D-ribose 1-phosphate (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:15205420};
CC Vmax=210 umol/min/mg enzyme (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:15205420};
CC Note=kcat is 173 sec(-1) (at 90 degrees Celsius).
CC {ECO:0000269|PubMed:15205420};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15205420};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.
CC {ECO:0000269|PubMed:15205420};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15205420}.
CC -!- PTM: Activated by phosphorylation. {ECO:0000250|UniProtKB:P31120}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB126239; BAD23919.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85966.1; -; Genomic_DNA.
DR RefSeq; WP_011250728.1; NC_006624.1.
DR AlphaFoldDB; Q6I7B6; -.
DR SMR; Q6I7B6; -.
DR STRING; 69014.TK1777; -.
DR EnsemblBacteria; BAD85966; BAD85966; TK1777.
DR GeneID; 3233830; -.
DR KEGG; tko:TK1777; -.
DR PATRIC; fig|69014.16.peg.1733; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR InParanoid; Q6I7B6; -.
DR OMA; VDCGNGM; -.
DR OrthoDB; 58941at2157; -.
DR PhylomeDB; Q6I7B6; -.
DR BRENDA; 5.4.2.7; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03087; PGM_like1; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR024086; GlmM_arc-type.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR TIGRFAMs; TIGR03990; Arch_GlmM; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..450
FT /note="Phosphopentomutase"
FT /id="PRO_0000433396"
FT ACT_SITE 93
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P31120"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 93
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P31120"
SQ SEQUENCE 450 AA; 49532 MW; A25A4A49D21862C8 CRC64;
MRLFGTAGIR GTLWEKVTPE LAMKVGMAVG TYKSGKALVG RDGRTSSVML KNAMISGLLS
TGMEVLDADL IPTPALAWGT RKLADAGVMI TASHNPPTDN GVKVFNGDGT EFYVEQERGL
EEIIFSGNFR KARWDEIKPV RNVEVIPDYI NAVLDFVGHE TNLKVLYDGA NGAGSLVAPY
LLREMGAKVL SVNAHVDGHF PGRKPEPRYE NIAYLGKLVR ELGVDLAIAQ DGDADRIAVF
DEKGNYVDED TVIALFAKLY VEEHGGGTVV VSIDTGSRID AVVERAGGRV VRIPLGQPHD
GIKRYKAIFA AEPWKLVHPK FGPWIDPFVT MGLLIKLIDE NGPLSELVKE IPTYYLKKAN
VLCPDEYKAE VVRRAAEEVE RKLSSEIKEV LTISGFRIAL NDGSWILIRP SGTEPKIRVV
AEAPTEKRRD ELFEMAYSTV SRIVKEAEKK
