ID G7N3Z3_MACMU Unreviewed; 262 AA.
AC G7N3Z3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00012730, ECO:0000256|RuleBase:RU361118};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730, ECO:0000256|RuleBase:RU361118};
GN ORFNames=EGK_03092 {ECO:0000313|EMBL:EHH20275.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH20275.1};
RN [1] {ECO:0000313|EMBL:EHH20275.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH20275.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(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|ARBA:ARBA00004699,
CC ECO:0000256|RuleBase:RU361118}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU361118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU361118}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family.
CC {ECO:0000256|ARBA:ARBA00009736, ECO:0000256|RuleBase:RU361118}.
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DR EMBL; CM001262; EHH20275.1; -; Genomic_DNA.
DR AlphaFoldDB; G7N3Z3; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000013456; Chromosome 10.
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 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:SF1; PHOSPHOMANNOMUTASE 1; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361118};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361118};
KW Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR605002-3}.
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 262 AA; 29733 MW; 4387CEE3BF854739 CRC64;
MAVTAQGSRR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYSKIA
EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR
LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR
FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV
VSPQDTVQRC REIFFPETAH EA
//
