ID   W0DEA2_9AQUI            Unreviewed;       455 AA.
AC   W0DEA2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AHE95363.1};
GN   ORFNames=THERU_00395 {ECO:0000313|EMBL:AHE95363.1};
OS   Thermocrinis ruber.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=75906 {ECO:0000313|Proteomes:UP000018914};
RN   [1] {ECO:0000313|EMBL:AHE95363.1, ECO:0000313|Proteomes:UP000018914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23557 {ECO:0000313|EMBL:AHE95363.1,
RC   ECO:0000313|Proteomes:UP000018914};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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; CP007028; AHE95363.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0DEA2; -.
DR   STRING; 75906.THERU_00395; -.
DR   KEGG; trd:THERU_00395; -.
DR   PATRIC; fig|75906.3.peg.74; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_1_0; -.
DR   Proteomes; UP000018914; 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; cd05800; PGM_like2; 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}.
FT   DOMAIN          2..134
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          150..249
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          257..366
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          403..451
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   455 AA;  50893 MW;  2BBF47624CB23975 CRC64;
     MRFGTDGWRA VIGEQFTFEN VRKVAYAHGL VLQEEGKKRV VVGYDRRFLS KEFAQEVCKV
     FLTLGLEAYL SEEECTTPMV SFGVKYLGFD GGVMITASHN PGKYNGYKIK ESFGGSAREE
     FVKKVEELAN RTQEVKVDNK KPELIDLKGP YIKKVQELIN LELFEEEDLL VHDAMHGSSA
     GLFSEALLNT PLSVVGIRTK RDPLFGGHPP EPIEKYLGPL FDKVRALGAR VGIANDGDGD
     RVALCDEKGN FVNTQLIYVL LLLHLLKNKG LKDGVVVKTV STSYLVDRIC RAEGVKLLEV
     PVGFKHINDV LFREKVIFGG EESGGYGIIH FLPERDGLFS GLSLLELLYT KGKSLSQIVE
     EVFETYGSAY YLRHDLHAEE EKKNKLKELI KNPPSQIGGF KVKEVITKDG LKLVFEGDGW
     LLLRASGTEP LIRVYVEMPT QEQAKEVLKS ALEML
//