PGMMM_THEKO
ID PGMMM_THEKO Reviewed; 456 AA.
AC Q68BJ6; Q5JE41;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000303|PubMed:15342576};
DE Short=PGM/PMM {ECO:0000303|PubMed:15342576};
DE EC=5.4.2.2 {ECO:0000269|PubMed:15342576};
DE EC=5.4.2.8 {ECO:0000269|PubMed:15342576};
GN OrderedLocusNames=TK1108 {ECO:0000312|EMBL:BAD85297.1};
GN ORFNames=Tko1621 {ECO:0000312|EMBL:BAD42440.1};
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], PROTEIN SEQUENCE OF 1-6, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP INDUCTION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15342576; DOI=10.1128/jb.186.18.6070-6076.2004;
RA Rashid N., Kanai T., Atomi H., Imanaka T.;
RT "Among multiple phosphomannomutase gene orthologues, only one gene encodes
RT a protein with phosphoglucomutase and phosphomannomutase activities in
RT Thermococcus kodakaraensis.";
RL J. Bacteriol. 186:6070-6076(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 interconversion of glucose 1-phosphate and
CC glucose 6-phosphate, and the interconversion of mannose 1-phosphate and
CC mannose 6-phosphate. Also displays low activity with deoxyribose 1-
CC phosphate and glucosamine 1-phosphate. {ECO:0000269|PubMed:15342576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000269|PubMed:15342576};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000269|PubMed:15342576};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15342576};
CC Note=Can also use Ni(2+), Mn(2+) and Zn(2+), to a lesser extent.
CC {ECO:0000269|PubMed:15342576};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 mM for glucose 1-phosphate {ECO:0000269|PubMed:15342576};
CC KM=3.2 mM for mannose 1-phosphate {ECO:0000269|PubMed:15342576};
CC KM=3.5 mM for 2-deoxyribose 1-phosphate
CC {ECO:0000269|PubMed:15342576};
CC Vmax=690 umol/min/mg enzyme with glucose 1-phosphate as substrate
CC {ECO:0000269|PubMed:15342576};
CC Vmax=401 umol/min/mg enzyme with mannose 1-phosphate as substrate
CC {ECO:0000269|PubMed:15342576};
CC Vmax=230 umol/min/mg enzyme with 2-deoxyribose 1-phosphate as
CC substrate {ECO:0000269|PubMed:15342576};
CC Note=kcat is 575 sec(-1) with glucose 1-phosphate as substrate. kcat
CC is 330 sec(-1) with mannose 1-phosphate as substrate. kcat is 190
CC sec(-1) with 2-deoxyribose 1-phosphate as substrate.
CC {ECO:0000269|PubMed:15342576};
CC pH dependence:
CC Optimum pH is 7.0 for PGM activity. {ECO:0000269|PubMed:15342576};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius for PGM activity.
CC {ECO:0000269|PubMed:15342576};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15342576}.
CC -!- INDUCTION: Up-regulated in the presence of starch.
CC {ECO:0000269|PubMed:15342576}.
CC -!- PTM: Activated by phosphorylation. {ECO:0000250|UniProtKB:P31120}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AB126241; BAD42440.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85297.1; -; Genomic_DNA.
DR RefSeq; WP_011250059.1; NC_006624.1.
DR AlphaFoldDB; Q68BJ6; -.
DR SMR; Q68BJ6; -.
DR STRING; 69014.TK1108; -.
DR EnsemblBacteria; BAD85297; BAD85297; TK1108.
DR GeneID; 3235711; -.
DR KEGG; tko:TK1108; -.
DR PATRIC; fig|69014.16.peg.1084; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR InParanoid; Q68BJ6; -.
DR OMA; PHNPEPL; -.
DR OrthoDB; 58941at2157; -.
DR PhylomeDB; Q68BJ6; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
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; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
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; PF02880; PGM_PMM_III; 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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..456
FT /note="Phosphoglucomutase/phosphomannomutase"
FT /id="PRO_0000433407"
FT ACT_SITE 101
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P31120"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 101
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P31120"
SQ SEQUENCE 456 AA; 49853 MW; 31DC72D11BE6FF06 CRC64;
MGKLFGTFGV RGIANEEITP EFALKIGMAF GTLLKREGRE RPLVVVGRDT RVSGEMLKDA
LISGLLSTGC DVIDVGIAPT PAIQWATNHF NADGGAVITA SHNPPEYNGI KLLEPNGMGL
KKEREAIVEE LFFSEDFHRA KWNEIGELRK EDIIKPYIEA IKNRVDVEAI KKRRPFVVVD
TSNGAGSLTL PYLLRELGCK VVSVNAHPDG HFPARNPEPN EENLKGFMEI VKALGADFGV
AQDGDADRAV FIDENGRFIQ GDKTFALVAD AVLRENGGGL LVTTIATSNL LDDIAKRNGA
KVMRTKVGDL IVARALLENN GTIGGEENGG VIFPDFVLGR DGAMTTAKIV EIFAKSGKKF
SELIDELPKY YQFKTKRHVE GDRKAIVAKV AELAEKKGYK IDTTDGTKII FDDGWVLVRA
SGTEPIIRIF SEAKSEEKAR EYLELGIKLL EEALKG
