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Database: UniProt
Entry: A0A2K9BKU7_9MOLU
LinkDB: A0A2K9BKU7_9MOLU
Original site: A0A2K9BKU7_9MOLU 
ID   A0A2K9BKU7_9MOLU        Unreviewed;       560 AA.
AC   A0A2K9BKU7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:AUF83856.1};
GN   ORFNames=CXP39_03635 {ECO:0000313|EMBL:AUF83856.1};
OS   Mesoplasma syrphidae.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC   Entomoplasmataceae; Mesoplasma.
OX   NCBI_TaxID=225999 {ECO:0000313|EMBL:AUF83856.1, ECO:0000313|Proteomes:UP000233419};
RN   [1] {ECO:0000313|EMBL:AUF83856.1, ECO:0000313|Proteomes:UP000233419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJS {ECO:0000313|EMBL:AUF83856.1,
RC   ECO:0000313|Proteomes:UP000233419};
RA   Knight T.F., Citino T., Rubinstein R., Neuschaefer Z.;
RT   "Mesoplasma syrphidae YJS, Complete Genome.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; CP025257; AUF83856.1; -; Genomic_DNA.
DR   RefSeq; WP_027048241.1; NZ_CP025257.1.
DR   AlphaFoldDB; A0A2K9BKU7; -.
DR   KEGG; msyr:CXP39_03635; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000233419; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233419}.
FT   DOMAIN          44..184
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          209..312
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          321..448
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          493..536
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   560 AA;  63977 MW;  22B3663E8FD4535C CRC64;
     MIYYKNNPVY KEWMESKSLE PQLKRMLQNA SEEELFAAFN LELEFGTAGI RGILGAGPGR
     FNLYTIRKVT ISYANLLIKK HFGRLKDGVV IGHDNRHNSA IFAQEVANIL TSFGITAYLF
     EDNKMKPTPV VSFATKALNC IGGVVITASH NPAEYNGYKI YDQFGCQLMP EDTDIIAAEM
     NKISNIIDWK YTPDIRLLKT VNKEITNKYL NMICNLEFYQ NHQSEKKMLK IVFSAVNGTG
     TEFTPVILKE SGYEVIEVAE HAYEDPTFEH VVNPNPEFDP AWKIPLQYGA KHNADLIILN
     DPDADRIGIA VKHNNKFYRL DGNQTGPILI DWKLKNLVRT NQMPINPVLY SSFVTSDLGD
     RIAHETYQTA IVKTLTGFKW MGNEMAKESV NGLNFVFAYE ESYGYVLDPS TRDKDGIQAS
     IMIAEACWFY KKQGQTLIDY LNELFLKYGY YYTETINLNF KPEEKDSKID PLMTSLRTDG
     LKQLNNLKVI KTEDYLDGLY NMPGQDLVKY YFEDGSWLAV RPSGTEPKLK IYFVTVGQNE
     KEAQAKTKTM YAELKKKMNI
//
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