ID   MANB_MYCPI              Reviewed;         544 AA.
AC   P47723;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=manB; Synonyms=cpsG;
OS   Mycoplasma pirum (Mycoplasmoides pirum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=2122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BER;
RX   PubMed=8349569; DOI=10.1128/jb.175.16.5281-5285.1993;
RA   Tham T.N., Ferris S., Kovacic R., Montagnier L., Blanchard A.;
RT   "Identification of Mycoplasma pirum genes involved in the salvage pathways
RT   for nucleosides.";
RL   J. Bacteriol. 175:5281-5285(1993).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; L13289; AAA25434.1; -; Genomic_DNA.
DR   PIR; E53312; E53312.
DR   AlphaFoldDB; P47723; -.
DR   SMR; P47723; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..544
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147829"
FT   ACT_SITE        145
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   544 AA;  62109 MW;  C4F8201F6D7887D0 CRC64;
     MNNEIVKKWL SSDNVPQTDK DIISKMKNEE LELAFSNAPL SFGTAGIRAK MAPGTQFLNK
     ITYYQMATGY GKFLKNKFSN QNISVIVAHD NRNNGIDFSI DVTNILTSLE LEFICLKIIN
     LLLRQLFSYA IRKLNAQGAV IVTASHNPKE DNGFKIYNET GAQVLPDDGL KVVELMPNVF
     EMIDLKVAND DSLITYLNED IFRQYYEDCK QALIKTNINE SKEFSIVFSG QHGTACKRLP
     EFLKLLGYKN IILVEEQCIF DGNFSNTPTP NPENRAAWDL SIEYADKNNA NVIIQVDPDA
     DRFALGVRYK NSWRFLSGNQ MGIIYTDYIL KNKTFTKKPY IVSSYVSTNL IDRIIKEYHG
     EVYRVGTGFK WVGDKINKIK DSEEFVVGFE EAVGALNSTI NRDKDAYQAA ALALEIYNEC
     LKNNINIIDH LEKNIYGKYG IIHNDTISFT FVENNWKELV KKSLDKILKY SEKTIGNRTI
     TSIKYNEVGG CYDWILDGDS WLRFRMSGTE PKFKVYYNLY GENLNALSQE AKTINDQIKT
     LLNL