ID   A0A0P0NIX4_9SPHI        Unreviewed;       577 AA.
AC   A0A0P0NIX4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ALL07125.1};
GN   ORFNames=AQ505_17510 {ECO:0000313|EMBL:ALL07125.1};
OS   Pedobacter sp. PACM 27299.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL07125.1, ECO:0000313|Proteomes:UP000062859};
RN   [1] {ECO:0000313|EMBL:ALL07125.1, ECO:0000313|Proteomes:UP000062859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL07125.1,
RC   ECO:0000313|Proteomes:UP000062859};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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; CP012996; ALL07125.1; -; Genomic_DNA.
DR   RefSeq; WP_062549363.1; NZ_CP012996.1.
DR   AlphaFoldDB; A0A0P0NIX4; -.
DR   STRING; 1727164.AQ505_17510; -.
DR   KEGG; pep:AQ505_17510; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000062859; 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:UP000062859}.
FT   DOMAIN          48..186
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          210..315
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          324..444
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          516..546
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   577 AA;  63706 MW;  79F15177D1398134 CRC64;
     MQLEAATLST INQWLNGNYD SKTKEEIQQL LDKEAFTELT DSFYRSLEFG TGGLRGIMGA
     GSNRINKYTI GTATQGLCNY LNNKYPNEKI KVAIAHDSRN NSDYFAGITA DVFTANGIHV
     YFFKALRPTP ELSFAIRELG CKSGVMLTAS HNPKEYNGYK AYGADGGQFT SPDDTMVMDE
     VAKIKNIDEV KFDRIDSNFE LIGEEIDQLY LDKITELSVS PEAIARQKDL KIVFSPIHGT
     GITLVPQALA QFGFTNLTLV EEQSTPDGNF PTVVYPNPEE KEALTLALKK AEEIDADLVL
     ATDPDADRVG IAVKNNDGQF VLLNGNQTGS LLINYLLSAW EEKGKLTGDQ YIVKTIVTTN
     IIEEIAKKKN VTFYNTLTGF KFIGQLMTSL EGKKTFIGGG EESYGYLIGE LVRDKDAVVS
     CAFIAEMTAF YKDKGSSLYN AMLDMYVEYG LYKEELVSIT KKGKTGAEEI KAMMEKFRSN
     PPATLGGAKV VLLKDYELGF ETNLSTAEKT KLDFPKSDVL QFITEDGSIV SARPSGTEPK
     IKFYCSVNTT LKDKASFKET DALLGDKIKA VMKDLEA
//