ID   MANB_MYCPN              Reviewed;         554 AA.
AC   P75050;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=manB; Synonyms=cpsG; OrderedLocusNames=MPN_066; ORFNames=MP088;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95736.1; -; Genomic_DNA.
DR   PIR; S73414; S73414.
DR   RefSeq; NP_109754.1; NC_000912.1.
DR   RefSeq; WP_010874423.1; NC_000912.1.
DR   AlphaFoldDB; P75050; -.
DR   SMR; P75050; -.
DR   IntAct; P75050; 3.
DR   STRING; 272634.MPN_066; -.
DR   EnsemblBacteria; AAB95736; AAB95736; MPN_066.
DR   KEGG; mpn:MPN_066; -.
DR   PATRIC; fig|272634.6.peg.67; -.
DR   HOGENOM; CLU_016950_0_0_14; -.
DR   OMA; PQDNGYK; -.
DR   BioCyc; MetaCyc:MON-621; -.
DR   BioCyc; MPNE272634:G1GJ3-103-MON; -.
DR   Proteomes; UP000000808; Chromosome.
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; IPR005843; A-D-PHexomutase_C.
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   Pfam; PF00408; PGM_PMM_IV; 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; Reference proteome.
FT   CHAIN           1..554
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147830"
FT   ACT_SITE        149
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  63215 MW;  9993A52B3D5E6C0B CRC64;
     MNSNAYLEAQ RWLSHPRVKP NLKEVITAMS AEEIEHFFSL KKPSFGTAGV RGKMAPGYHG
     MNVFSYAYLT QGYVNYIQSL NPTKKPLRFL VARDTRKHGA LFNGIVCDVI TSMGHVVYMF
     DNNEPTPTPL VSYVIKKYHF DGGVNVTASH NPKTDNGFKI YDGHGAQLLD FQTDQLIAML
     PPVVTMLDFE PRGNNELLHF LDNEVVYKNY FDDLKESLVV DNDSFKNLPV VFTGLHGTSV
     KLLPRFLTYL GYSNIISVQP QNVFDANFAN ADHLNPESKD TWELARQYAS NTKAKLMMAI
     DPDADRFAIA EWNPQTQDWH YFSGNESGVM VAYYKLKHKQ FKRQPYIVTT VVSTDLVDKI
     AKKYGAFVKR TNVGFKFIGQ AVNHFSKDNE LVVAFEEAIG MMASDGLNRE KDSFQAAAIM
     LEIARYCHNK GISLLEFYRG EIFGEFGDYY NWTVPHTIHG VNWKEKMEQV LHQLTTATIK
     EVVGHKITKI KNYVDINLVE YVLENGNWIK FRISGTEPKL KLYFNLSNGY LAALKHEAKK
     MHEFLVRLLN LDKA