ID NOEK_SINFN Reviewed; 474 AA.
AC P55356;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Phosphomannomutase;
DE Short=PMM;
DE EC=5.4.2.8;
GN Name=noeK; OrderedLocusNames=NGR_a00390; ORFNames=y4aI;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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; U00090; AAB91606.1; -; Genomic_DNA.
DR RefSeq; NP_443768.1; NC_000914.2.
DR RefSeq; WP_010875081.1; NC_000914.2.
DR AlphaFoldDB; P55356; -.
DR SMR; P55356; -.
DR KEGG; rhi:NGR_a00390; -.
DR PATRIC; fig|394.7.peg.37; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_045514_1_0_5; -.
DR OrthoDB; 9803322at2; -.
DR PRO; PR:P55356; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
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 CDD; cd03088; ManB; 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 PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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 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; Nodulation; Phosphoprotein; Plasmid;
KW Reference proteome.
FT CHAIN 1..474
FT /note="Phosphomannomutase"
FT /id="PRO_0000147833"
FT ACT_SITE 101
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 49671 MW; 6965310CEA96A22B CRC64;
MGPKFGTSGL RGLATELVGS VSALYATAFS RMLLDRGRVA PGATVLVGRD FRDSSSEIAA
ICMAALARAG MVPVDCGGLP TPALALYGRK LGAASLMITG SHIPADRNGI KFYLPDGEIN
KADEQAITAL AEQLSADADA TRVECGRGAD HSSEATDFYI QRYETLLPKS GLKGLKIGLY
QHSSVARDIL TTILEGHGAN VVPVGRSEVF IPVDTEAISA ATCKMLAAWA KEFAFDAIVS
SDADADRPLL TDETGTPLRG DLLGLICARL LEAKLIATPI TSNSGIEAAS GVEVVRTRVG
SPYVIAAMTE AVARGKQRVM GFEANGGVML GSNFSFGGAS LPALPTRDCV LPIIAALHMA
VEAKTPLSGI VAMHRLPVAL SGRIENYPFD RSDALVAFLK ASKANVSHLF SRIGRVAGTD
DVDGLRLTFE GGRILHIRPS GNAPELRCYV EADDPDAAEH LLAQGLAVLN SSMV
//
