ID U3DRA6_CALJA Unreviewed; 262 AA.
AC U3DRA6; H9KVU6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 Name=PMM1 {ECO:0000313|EMBL:JAB34742.1,
GN ECO:0000313|Ensembl:ENSCJAP00000004680.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB34742.1};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000004680.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB34742.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB08800.1}, Cerebellum
RC {ECO:0000313|EMBL:JAB43700.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB24267.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB18758.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB34742.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000004680.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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}.
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; GAMT01003061; JAB08800.1; -; mRNA.
DR EMBL; GAMS01004378; JAB18758.1; -; mRNA.
DR EMBL; GAMR01009665; JAB24267.1; -; mRNA.
DR EMBL; GAMQ01007109; JAB34742.1; -; mRNA.
DR EMBL; GAMP01009055; JAB43700.1; -; mRNA.
DR RefSeq; XP_002763952.1; XM_002763906.3.
DR STRING; 9483.ENSCJAP00000004680; -.
DR Ensembl; ENSCJAT00000004937.4; ENSCJAP00000004680.3; ENSCJAG00000002559.5.
DR GeneID; 100391103; -.
DR KEGG; cjc:100391103; -.
DR CTD; 5372; -.
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_1_0_1; -.
DR OMA; EKTIGHT; -.
DR OrthoDB; 167037at2759; -.
DR TreeFam; TF300874; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000008225; Chromosome 1.
DR Bgee; ENSCJAG00000002559; Expressed in kidney and 6 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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 GO; GO:0006013; P:mannose metabolic process; IEA:Ensembl.
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; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 2: Evidence at transcript level;
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|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR605002-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225}.
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; 29743 MW; 43811C29BF8AE6E3 CRC64;
MAVTPQGARR 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
//