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Database: UniProt
Entry: G3II51_CRIGR
LinkDB: G3II51_CRIGR
Original site: G3II51_CRIGR 
ID   G3II51_CRIGR            Unreviewed;       118 AA.
AC   G3II51;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Phosphomannomutase {ECO:0000256|RuleBase:RU361118};
DE            EC=5.4.2.8 {ECO:0000256|RuleBase:RU361118};
GN   ORFNames=I79_023513 {ECO:0000313|EMBL:EGW13957.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW13957.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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:0000256|RuleBase:RU361118}.
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:0000256|RuleBase:RU361118};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR605002-3};
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:0000256|RuleBase:RU361118}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361118}.
CC   -!- SIMILARITY: Belongs to the eukaryotic PMM family.
CC       {ECO:0000256|RuleBase:RU361118}.
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DR   EMBL; JH002929; EGW13957.1; -; Genomic_DNA.
DR   RefSeq; XP_003514361.1; XM_003514313.3.
DR   AlphaFoldDB; G3II51; -.
DR   STRING; 10029.G3II51; -.
DR   GeneID; 100771643; -.
DR   CTD; 5372; -.
DR   InParanoid; G3II51; -.
DR   OMA; DVFPPGW; -.
DR   OrthoDB; 167037at2759; -.
DR   UniPathway; UPA00126; UER00424.
DR   Proteomes; UP000001075; 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; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005002; PMM.
DR   PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR10466:SF1; PHOSPHOMANNOMUTASE 1; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU361118};
KW   Isomerase {ECO:0000256|RuleBase:RU361118};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR605002-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ   SEQUENCE   118 AA;  13433 MW;  00737677CAF28B5A CRC64;
     MGPLSQYAPF FPAQKEKIRE KFVEALKTEF AGKGLRFSRG GMISFDVFPE GWDKRYCLDS
     LDEDSFDIIH FFGNETSPGG NDFEIYADPR TVGHSVVSPQ DTVQRCRELF FPETAHEA
//
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