ID   MANB_MYCGE              Reviewed;         550 AA.
AC   P47299; Q49247;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=manB; Synonyms=cpsG; OrderedLocusNames=MG053;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD12379.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L43967; AAC71269.1; -; Genomic_DNA.
DR   EMBL; U02108; AAD12379.1; ALT_INIT; Genomic_DNA.
DR   PIR; H64205; H64205.
DR   RefSeq; WP_009885715.1; NZ_AAGX01000003.1.
DR   AlphaFoldDB; P47299; -.
DR   SMR; P47299; -.
DR   STRING; 243273.MG_053; -.
DR   KEGG; mge:MG_053; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_14; -.
DR   InParanoid; P47299; -.
DR   OrthoDB; 9806956at2; -.
DR   BioCyc; MGEN243273:G1GJ2-54-MONOMER; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IBA:GO_Central.
DR   CDD; cd05799; PGM2; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..550
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147828"
FT   ACT_SITE        148
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        42..46
FT                   /note="PLFGT -> LYLAL (in Ref. 2; AAD12379)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  63397 MW;  D7BDF8920923508D CRC64;
     MDKLRLEVER WLNHPNVNWE LKQQIKELNE SEIQELFSLE KPLFGTAGVR NKMAPGYHGM
     NVFSYAYLTQ GYVKYIESIN EPKRQLRFLV ARDTRKNGGL FLETVCDVIT SMGHLAYVFD
     DNQPVSTPLV SHVIFKYGFS GGINITASHN PKDDNGFKVY DHTGAQLLDT QTNQLLSDLP
     CVTSMLDLEL QPNPKFVHTL DNEKVYKNYF RELKKVLVIN NNNFKDIKVV FSGLNGTSVC
     LMQRFLKYLG YSNIISVEEQ NWFDENFENA PNLNPEYKDT WILAQKYAKK NNAKLIIMAD
     PDADRFAIAE LNNNQWHYFS GNETGAITAY YKLNHKVFKS PYIVSTFVST YLVNKIAKRY
     GAFVHRTNVG FKYIGQAINE LSQTNELVVG FEEAIGLITS DKLNREKDAY QAAALLLEIA
     RHCKEQNITL LDFYKRILSE FGEYFNLTIS HPFKATATDW KEEIKALFNQ LINANLTEVA
     GFKVVKVHLD KQTNILEFGF ENGWVKFRFS GTEPKLKFYF DLTNGTREAL EKQAKKIYKF
     FVNLLKLNKA
//