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Database: UniProt
Entry: A0A0J8UMI0_COCIT
LinkDB: A0A0J8UMI0_COCIT
Original site: A0A0J8UMI0_COCIT 
ID   A0A0J8UMI0_COCIT        Unreviewed;       245 AA.
AC   A0A0J8UMI0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=CIHG_06416 {ECO:0000313|EMBL:KMU88748.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU88748.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; DS017007; KMU88748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8UMI0; -.
DR   STRING; 396776.A0A0J8UMI0; -.
DR   VEuPathDB; FungiDB:CIHG_06416; -.
DR   eggNOG; KOG3189; Eukaryota.
DR   UniPathway; UPA00126; UER00424.
DR   Proteomes; UP000054563; 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   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   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|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR605002-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054563}.
FT   BINDING         206
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         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ   SEQUENCE   245 AA;  27943 MW;  F891ED28D6F0311F CRC64;
     MPVPAHPGHC ATVRRSSRLL STDMYDLPIP QVGGSDLAKQ QEQLGSQTTS VTSLFDFCFA
     ENGLVAFRMG QPLKSNSFIQ WLGEEKYQKL VDFCLRYIAD LRLPKKRGTF VEFRNGMVNI
     SPIGRNASTQ ERLDFQEYDK VHNIRKTMVE ALKKEFPDYG LTYSIGGQIS FDVFPNGWDK
     TYCLQHVEAE KNISGVEFST IHFFGDKAFE GGNDWEIYID KRTTGHAVNT PEDTMKLLRD
     MFDLN
//
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