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Database: UniProt
Entry: C3KRY6_SINFN
LinkDB: C3KRY6_SINFN
Original site: C3KRY6_SINFN 
ID   C3KRY6_SINFN            Unreviewed;       518 AA.
AC   C3KRY6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:ACP22844.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:ACP22844.1};
GN   Name=manB {ECO:0000313|EMBL:ACP22844.1};
GN   OrderedLocusNames=NGR_b13930 {ECO:0000313|EMBL:ACP22844.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234b {ECO:0000313|Proteomes:UP000001054}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP22844.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=14702322; DOI=10.1128/JB.186.2.535-542.2004;
RA   Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., Raasch C.,
RA   Liesegang H., Broughton W.J.;
RT   "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. strain
RT   NGR234.";
RL   J. Bacteriol. 186:535-542(2004).
RN   [2] {ECO:0000313|EMBL:ACP22844.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; CP000874; ACP22844.1; -; Genomic_DNA.
DR   RefSeq; WP_015887485.1; NC_012586.1.
DR   RefSeq; YP_002823597.1; NC_012586.1.
DR   AlphaFoldDB; C3KRY6; -.
DR   KEGG; rhi:NGR_b13930; -.
DR   PATRIC; fig|394.7.peg.1796; -.
DR   HOGENOM; CLU_016950_9_1_5; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234b.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ACP22844.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:ACP22844.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN          40..177
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          195..291
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          297..407
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          447..505
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  56378 MW;  F5C641F77EF87CCC CRC64;
     MAQVEFARID PGSSYEPLHE SGPDRFTLET SALIRPTGFR EYDARWWFGR PDDGKAPDLN
     LMGVQALGMG LGTFMRRSGA GPEIVTGHDF RSYSLGIKLA LVSGLLAAGA RVRDIGLALS
     PMAYFAQFAL DVPSVAMVTA SHNENGWTGV KMGTARPLTF GPDEMAELKR IVLEADFDLT
     GGGAYEFIAD FRQRYIDDLT RDRRIARKLK VVVACGNGTA GAFAPHVLER IGCEVIPLDC
     ELDHSFPHYN PNPEDLAMLH AIRDKVLESG ADVGLGFDGD GDRCGVVDNE GREIFADKIG
     VMLARDLSAL HPNSVFVVDV KSTGLFASDP VLKASGAHTD YWKTGHSYIK RRVAELGALA
     GFEKSGHFFF NPPLGRGYDD GLITALAVCE MLDRNPGMSM AELYRSLPVT WGSPTMSPHC
     DDEVKYAVVE RVVERFRTMQ RDGLPVAGQQ IANLVTVNGV RVVVEDGTWG LVRASSNKPE
     LVVVVESPVS EARQRAMFAA VDGVLREHAE VGAYNQTI
//
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