PMM_GALSU
ID PMM_GALSU Reviewed; 251 AA.
AC M2VWL5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:9003801};
DE EC=5.4.2.8 {ECO:0000269|PubMed:9003801};
GN Name=PMM {ECO:0000305}; ORFNames=Gasu_47860 {ECO:0000312|EMBL:EME27641.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Galdieria.
OX NCBI_TaxID=130081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W;
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9003801; DOI=10.1016/s0014-5793(96)01425-1;
RA Oesterhelt C., Schnarrenberger C., Gross W.;
RT "The reaction mechanism of phosphomannomutase in plants.";
RL FEBS Lett. 401:35-37(1997).
CC -!- FUNCTION: Catalyzes the interconversion of mannose-6-phosphate to
CC mannose-1-phosphate, the precursor for the synthesis of GDP-mannose
CC (PubMed:9003801). GDP-mannose is an essential sugar nucleotide for the
CC synthesis of D-mannose-containing cell wall polysaccharides
CC (galactomannans and glucomannans), glycolipids, glycoproteins and the
CC antioxidant L-ascorbate (Probable). {ECO:0000269|PubMed:9003801,
CC ECO:0000305}.
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:9003801};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q92871};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for glucose-1-phosphate {ECO:0000269|PubMed:23471408};
CC KM=4 uM for mannose-1-phosphate {ECO:0000269|PubMed:23471408};
CC Note=Glucose-1,6-bisphosphate or mannose-1,6-biphosphate are
CC essential for activity. {ECO:0000269|PubMed:9003801};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2. {ECO:0000269|PubMed:9003801, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q92871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A0U1WZ18}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family.
CC {ECO:0000269|PubMed:9003801}.
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; KB454529; EME27641.1; -; Genomic_DNA.
DR RefSeq; XP_005704161.1; XM_005704104.1.
DR AlphaFoldDB; M2VWL5; -.
DR SMR; M2VWL5; -.
DR STRING; 130081.XP_005704161.1; -.
DR EnsemblPlants; EME27641; EME27641; Gasu_47860.
DR GeneID; 17086531; -.
DR Gramene; EME27641; EME27641; Gasu_47860.
DR KEGG; gsl:Gasu_47860; -.
DR eggNOG; KOG3189; Eukaryota.
DR OMA; VCPIGRQ; -.
DR OrthoDB; 1038583at2759; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IDA:UniProtKB.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IDA:UniProtKB.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005002; PMM.
DR InterPro; IPR043169; PMM_cap.
DR PANTHER; PTHR10466; PTHR10466; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..251
FT /note="Phosphomannomutase"
FT /id="PRO_0000451445"
FT ACT_SITE 18
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT ACT_SITE 20
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 27
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 129
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 140
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 147
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 185
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 187
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
SQ SEQUENCE 251 AA; 29017 MW; F89F18C1154BF2A9 CRC64;
MSHIRRMPKR TDTLALFDVD GTLTPSRCKA SHETLEFLRR LRDEVFTGIV GGSDLVKQEE
QLGPTILEDF DYVFSENGLV AYEKGKLIHV QSLAKHLGEE KLKNVINCCL RYIADLDIPL
KRGTFVEFRK GMLNVSPIGR NCSQQEREEF EKYDRVHSIR SRFVDYLKER FEGYDLQFSI
GGQISFDVFP RGWDKTYCLS FVKHIPVIHF FGDKTFLGGN DYEIFQDART IGHSVTSPED
TVKQCQQLFN L
