MANB_MYCGE
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 03-AUG-2022, entry version 119.
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; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PRIDE; P47299; -.
DR EnsemblBacteria; AAC71269; AAC71269; MG_053.
DR KEGG; mge:MG_053; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_14; -.
DR OMA; PQDNGYK; -.
DR OrthoDB; 637615at2; -.
DR BioCyc; MGEN243273:G1GJ2-54-MON; -.
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 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 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; 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..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
