ID   A0A3Q8T368_9RICK        Unreviewed;       470 AA.
AC   A0A3Q8T368;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:AZL16413.1};
GN   ORFNames=EF513_07755 {ECO:0000313|EMBL:AZL16413.1};
OS   Rickettsiales endosymbiont of Stachyamoeba lipophora.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX   NCBI_TaxID=2486578 {ECO:0000313|EMBL:AZL16413.1, ECO:0000313|Proteomes:UP000267655};
RN   [1] {ECO:0000313|EMBL:AZL16413.1, ECO:0000313|Proteomes:UP000267655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RICK01 {ECO:0000313|EMBL:AZL16413.1,
RC   ECO:0000313|Proteomes:UP000267655};
RA   Munoz-Gomez S.A., Hess S., Burger G., Lang B.F., Susko E., Slamovits C.H.,
RA   Roger A.J.;
RT   "An updated phylogeny of the Alphaproteobacteria reveals that the parasitic
RT   Rickettsiales and Holosporales have independent origins.";
RL   Submitted (NOV-2018) 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; CP033611; AZL16413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q8T368; -.
DR   KEGG; ren:EF513_07755; -.
DR   Proteomes; UP000267655; 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; 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; IPR016066; A-D-PHexomutase_CS.
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.
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:UP000267655}.
FT   DOMAIN          14..145
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          164..262
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          267..376
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          382..458
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   470 AA;  52105 MW;  86AF22F2C195F747 CRC64;
     MSGHSSYSHY INPQCFREYD IRGEIGQNLF SQDAYYIGKA IASYVIDNSN NYRICIGCDG
     RLTSPVLEST LIDGIKSCGV DVISIGVCPT PMLYYATHST DSPHGVMITG SHNPADHNGF
     KIVINKKPFF GDKIQKLYET IAKADYRTTG KNAVKIVDLK VNEAYTATVA NGLNFAKKFL
     KVAWDPGHGS SADIVNKLVE KLPGKHFVIN NYIDGNFPAH DPDPTNPKNL IQLGEIIKKE
     KCDLGIAFDG DADRLVALDH KGRMLSGDAL IAIFARSILN KSPKARIITD IKASKTIIDY
     INDNGGIALM WKTGHSNIKE KMQEIGAIMA GEVSGHIFFA DKYYGYDDGL YAAVRLIEII
     ANSEKDLAEL VNELPKTIIT PEVRIECADE RKFQVINEIK ERLKQEDKKY LDIDGIRAES
     KGGWWLIRAS NTQAALVIRF EASTEEELVA LQQEVKQQLI LSKVTVSIAL
//