ID   X5DZR1_9BACT            Unreviewed;       580 AA.
AC   X5DZR1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SEU01957.1};
GN   ORFNames=SAMN05444285_13552 {ECO:0000313|EMBL:SEU01957.1};
OS   Draconibacterium orientale.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Draconibacterium.
OX   NCBI_TaxID=1168034 {ECO:0000313|EMBL:SEU01957.1, ECO:0000313|Proteomes:UP000181981};
RN   [1] {ECO:0000313|EMBL:SEU01957.1, ECO:0000313|Proteomes:UP000181981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25947 {ECO:0000313|EMBL:SEU01957.1,
RC   ECO:0000313|Proteomes:UP000181981};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOHT01000035; SEU01957.1; -; Genomic_DNA.
DR   RefSeq; WP_038560971.1; NZ_FOHT01000035.1.
DR   AlphaFoldDB; X5DZR1; -.
DR   STRING; 1168034.FH5T_16780; -.
DR   GeneID; 78101163; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_10; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000181981; Unassembled WGS sequence.
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}.
FT   DOMAIN          50..188
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          221..316
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          327..450
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          515..555
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   580 AA;  64907 MW;  70CF81210759EA13 CRC64;
     MENQELMEVR AKAQEWLSDT YDEETRAQVQ ALLDAEDPTE LIDSFYRSLE FGTGGLRGIM
     GVGTNRMNIY TVGAATQGLS NYLKKNFADL DEIKVAIGHD CRNNSRLFSE TSAKIFAANG
     IKAYLFEDLR PTPELSFAIR ERGCQSGIIL TASHNPKEYN GYKAYWEDGS QIVAPHDVNI
     VNEVAKIKPE DIKFDGSDDL IEILGEEMDN KFLAEVKKVS ISPDVVERHK DIKIIYTPIH
     GTGVKLIPAA LREFGFTNII NIPEQDVVSG DFPTVVSPNP EEPAAMEMAT KKAAEIDADV
     VMASDPDSDR IGVAVKNDKG EYIIVNGNQT ALLFFYYIIV KMKEAGKLKG NEFVVKTIVS
     TEMIAEVARR NNIEYFDVYT GFKFIAEVIR DNEGVKKYIG GGEESFGFMP SDFVRDKDAV
     SACALMAEIT AWAIDQGKTL YELLQDIYLE YGFSREKMKY VVRKGKSGAE EIQQIMTKFR
     NDPPKELGGS PMEWVKDYST LIAKNLITGE EKKIDQKVTS NVLQFFTQDG TKISVRPSGT
     EPKIKFYFEV AGELKSREDF DAEEQKADAK IDAIMEELGL
//