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Database: UniProt
Entry: A0A0L8G8R5_OCTBM
LinkDB: A0A0L8G8R5_OCTBM
Original site: A0A0L8G8R5_OCTBM 
ID   A0A0L8G8R5_OCTBM        Unreviewed;       141 AA.
AC   A0A0L8G8R5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=OCBIM_22037884mg {ECO:0000313|EMBL:KOF73431.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF73431.1};
RN   [1] {ECO:0000313|EMBL:KOF73431.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF73431.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF73431.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ423143; KOF73428.1; -; Genomic_DNA.
DR   EMBL; KQ423143; KOF73429.1; -; Genomic_DNA.
DR   EMBL; KQ423143; KOF73430.1; -; Genomic_DNA.
DR   EMBL; KQ423143; KOF73431.1; -; Genomic_DNA.
DR   EnsemblMetazoa; Ocbimv22037880m; Ocbimv22037880m.p; Ocbimv22037884m.g.
DR   EnsemblMetazoa; Ocbimv22037881m; Ocbimv22037881m.p; Ocbimv22037884m.g.
DR   EnsemblMetazoa; Ocbimv22037882m; Ocbimv22037882m.p; Ocbimv22037884m.g.
DR   EnsemblMetazoa; Ocbimv22037883m; Ocbimv22037883m.p; Ocbimv22037884m.g.
DR   EnsemblMetazoa; XM_014927616.1; XP_014783102.1; LOC106878409.
DR   UniPathway; UPA00126; UER00424.
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; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005002; PMM.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR10466:SF14; PHOSPHOMANNOMUTASE; 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|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361118};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR605002-3}.
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ   SEQUENCE   141 AA;  16442 MW;  4265F54A306E0008 CRC64;
     MSTIRLPCKR GTFIEFRKSM LNFCPIGRSC SQTERDAFSK YDQEHQVRKK FVNALYERFP
     DLGLHYVIGG QISIDVIPEG WNKSYCLKYV ERDGFKTIHF FGDKTQPGGN DHEIYEDKRT
     IGHMVKNPDD TIQQLNELFL G
//
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