ID   PMM_BABBO               Reviewed;         246 AA.
AC   O43976; O15780;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Phosphomannomutase;
DE            EC=5.4.2.8;
GN   Name=PMM;
OS   Babesia bovis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5865;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Mexico Mo7;
RX   PubMed=9662706; DOI=10.1016/s0166-6851(98)00032-2;
RA   Suarez C.E., Palmer G.H., Hotzel I., McElwain T.F.;
RT   "Structure, sequence, and transcriptional analysis of the Babesia bovis
RT   rap-1 multigene locus.";
RL   Mol. Biochem. Parasitol. 93:215-224(1998).
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:0000250}.
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;
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.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR   EMBL; AF027149; AAC27385.1; -; Genomic_DNA.
DR   EMBL; AF028591; AAC27390.1; -; mRNA.
DR   AlphaFoldDB; O43976; -.
DR   SMR; O43976; -.
DR   STRING; 5865.XP_001610907.1; -.
DR   VEuPathDB; PiroplasmaDB:BBOV_IV009850; -.
DR   eggNOG; KOG3189; Eukaryota.
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   CDD; cd02585; HAD_PMM; 1.
DR   Gene3D; 3.30.1240.20; -; 1.
DR   Gene3D; 3.40.50.1000; -; 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   PANTHER; PTHR10466; PTHR10466; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..246
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000199697"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   ACT_SITE        11
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         121
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         132
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         139
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         179
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         181
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P31353"
SQ   SEQUENCE   246 AA;  28167 MW;  3A0FC96439CF0A80 CRC64;
     MVRQMLIFDM DGTLTDPVQV INNDVKDILR RCKRKNFEIA VVSGSKYEKI KGQLNDGFID
     EFDYVFSENG TQVYVKNVLV KSLDITEAIP ETKLRKMVEF CLRYIADLDI PTKRGTFIEH
     RKSLINICPP GRNCSMVDRR RFVEYDSIHH VRQKLIQVLK SQFDSDDCPL SFVAGGQISI
     DVYPKAWSKS IALSHIGKCD VIHFFGDNTR EGGNDFEIYN HPDVIGHTVT GYKDLVNQLE
     ELLAKS