ID   A0A2T3HKH8_9SPHI        Unreviewed;       577 AA.
AC   A0A2T3HKH8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:PST82913.1};
GN   ORFNames=C7T94_09775 {ECO:0000313|EMBL:PST82913.1};
OS   Pedobacter yulinensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=2126353 {ECO:0000313|EMBL:PST82913.1, ECO:0000313|Proteomes:UP000240912};
RN   [1] {ECO:0000313|EMBL:PST82913.1, ECO:0000313|Proteomes:UP000240912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL28-9 {ECO:0000313|EMBL:PST82913.1,
RC   ECO:0000313|Proteomes:UP000240912};
RA   Keele B.F.;
RL   Submitted (MAR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PST82913.1}.
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DR   EMBL; PYLS01000005; PST82913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3HKH8; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000240912; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240912}.
FT   DOMAIN          48..185
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          324..443
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          516..545
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   577 AA;  63584 MW;  F7FAA41AFDCF8244 CRC64;
     MALEQNVQEG IDQWLQGNYD EETKQQIRGL IDANAETELT DSFYKSLEFG TGGLRGIMGP
     GSNRINKYTI GTATQGLCNY LLSKYPGQRI SVAIAHDSRN NSDYFAKITA DVFSANGIFV
     YFFSELRPTP ELSFAIRQLG CKSGVMLTAS HNPKEYNGYK AYGPDGGQFT SPDDKLVIAE
     VNKIGSIDEV RFERVDENIQ FILEDIDNRY LDAITALSVS PEAIGRQKEL KIVYSPIHGT
     GITLVPKALS RFGFTNVHVV EEQSQPDGNF PTVVYPNPEE KEAMTLALRK AAEIDADLVL
     ATDPDADRVG IAVKNLEGEF VLLNGNQTGS LLINYLLSAW EEKGKLDGNQ YIVKTIVTSN
     LIEAIASKKQ VKYYNTLTGF KYIGQLMTEL EGKAYFIGGG EESYGYLVGD LVRDKDAVVS
     AAFIAEMTAF YKDKGSSLFE ALIGMYEEYG FYKEELVSIT KKGKSGAEEI KALMEKFRNN
     PPATLGGSAV LTLKDYEQGI ETDLQTKTTR QLELPKSDVL QFITEDGSIV SARPSGTEPK
     IKFYCSVNTS LPDSTAFAAT DRQLSEKIDS VMKDLGV
//