ID   P74643_SYNY3            Unreviewed;       567 AA.
AC   P74643;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 159.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:BAA18759.1};
GN   Name=pgm {ECO:0000313|EMBL:BAA18759.1};
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA18759.1, ECO:0000313|Proteomes:UP000001425};
RN   [1] {ECO:0000313|EMBL:BAA18759.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa
RC   {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2] {ECO:0000313|EMBL:BAA18759.1, ECO:0000313|Proteomes:UP000001425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa
RC   {ECO:0000313|Proteomes:UP000001425};
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- INTERACTION:
CC       P74643; P52231: trxA; NbExp=2; IntAct=EBI-862197, EBI-862916;
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; BA000022; BAA18759.1; -; Genomic_DNA.
DR   PIR; S76847; S76847.
DR   AlphaFoldDB; P74643; -.
DR   SMR; P74643; -.
DR   IntAct; P74643; 4.
DR   STRING; 1148.gene:10500531; -.
DR   PaxDb; 1148-gene:10500531; -.
DR   EnsemblBacteria; BAA18759; BAA18759; BAA18759.
DR   KEGG; syn:sll0726; -.
DR   eggNOG; COG0033; Bacteria.
DR   InParanoid; P74643; -.
DR   PhylomeDB; P74643; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05801; PGM_like3; 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; IPR045244; PGM.
DR   InterPro; IPR005852; PGM_a-D-Glc-sp.
DR   NCBIfam; TIGR01132; pgm; 1.
DR   PANTHER; PTHR22573:SF57; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   1: Evidence at protein level;
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:UP000001425}.
FT   DOMAIN          59..201
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          232..337
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          343..461
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          506..557
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   567 AA;  61125 MW;  21B0471FAA87A1DB CRC64;
     MSKPLIAALH FLQFLYMTSR INPLAGQHPP ADSLLDVAKL LDDYYRQQPD PENPAQLVSF
     GTSGHRGSAL NGTFNEAHIL AVTQAVVDYR QAQGITGPLY MGMDSHALSE PAQKTALEVL
     AANQVETFLT TATDLTRFTP TPAVSYAILT HNQGRKEGLA DGIIITPSHN PPTDGGFKYN
     PPSGGPAEPE ATQWIQNRAN ELLKNGNKTV KRLDYEQALK ATTTHAHDFV TPYVAGLADI
     IDLDVIRSAG LRLGVDPLGG ANVGYWEPIA AKYNLNISLV NPGVDPTFKF MTLDWDGKIR
     MDCSSPYAMA SLVKIKDHYD IAFGNDTDGD RHGIVTPSVG LMNPNHFLSV AIWYLFSQRQ
     QWSGLSAIGK TLVSSSMIDR VGAMINRQVY EVPVGFKWFV SGLLDGSFGF GGEESAGASF
     LKKNGTVWTT DKDGTIMDLL AAEITAKTGK DPGLHYQDLT AKLGNPIYQR IDAPATPAQK
     DRLKKLSPDD VTATSLAGDA ITAKLTKAPG NQAAIGGLKV TTAEGWFAAR PSGTENVYKI
     YAESFKDEAH LQAIFTEAEA IVTSALG
//