ID   PMM1_DICDI              Reviewed;         249 AA.
AC   Q54X03;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Phosphomannomutase 1;
DE            Short=PMM 1;
DE            EC=5.4.2.8;
GN   Name=pmmA; ORFNames=DDB_G0279289;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC       phosphate-mannose required for a number of critical mannosyl transfer
CC       reactions. {ECO:0000250}.
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;
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.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR   EMBL; AAFI02000030; EAL67793.1; -; Genomic_DNA.
DR   RefSeq; XP_641774.1; XM_636682.1.
DR   AlphaFoldDB; Q54X03; -.
DR   SMR; Q54X03; -.
DR   STRING; 44689.Q54X03; -.
DR   PaxDb; 44689-DDB0231660; -.
DR   EnsemblProtists; EAL67793; EAL67793; DDB_G0279289.
DR   GeneID; 8621971; -.
DR   KEGG; ddi:DDB_G0279289; -.
DR   dictyBase; DDB_G0279289; pmmA.
DR   eggNOG; KOG3189; Eukaryota.
DR   HOGENOM; CLU_065642_0_0_1; -.
DR   InParanoid; Q54X03; -.
DR   OMA; ISHRVYT; -.
DR   PhylomeDB; Q54X03; -.
DR   Reactome; R-DDI-446205; Synthesis of GDP-mannose.
DR   UniPathway; UPA00126; UER00424.
DR   PRO; PR:Q54X03; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   CDD; cd02585; HAD_PMM; 1.
DR   Gene3D; 3.30.1240.20; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR10466:SF0; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..249
FT                   /note="Phosphomannomutase 1"
FT                   /id="PRO_0000327516"
FT   ACT_SITE        12
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   ACT_SITE        14
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         21
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         123
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         134
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         141
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         179
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         181
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P31353"
FT   BINDING         223
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"
SQ   SEQUENCE   249 AA;  28558 MW;  1490BEAA64356233 CRC64;
     MSLVPNTICL FDVDGTLTKP RNVITPEMKD FLAGLRTKVE LGVVGGSDIN KIKEQLGENC
     INEFHYLFAE NGLLSFKDGS LLATQDIKKF LGEENIKKFI NFVLHYIADL DIPIKRGTFV
     EFRNGMINIS PIGRNCSQQE REEFEKYDLE HKIRPTMVSI LKEKFQSLGL QYSIGGQISF
     DVFPIGWDKT YCLRHLPEDK YKTIYFFGDK TFVGGNDYEI ANDPRITKSF TVTSPTDTKN
     FLSELFYKQ
//