ID I4IEE2_9CHRO Unreviewed; 544 AA.
AC I4IEE2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN Name=pgm {ECO:0000313|EMBL:CCI32666.1};
GN ORFNames=MICAI_270008 {ECO:0000313|EMBL:CCI32666.1};
OS Microcystis sp. T1-4.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1160279 {ECO:0000313|EMBL:CCI32666.1, ECO:0000313|Proteomes:UP000004501};
RN [1] {ECO:0000313|EMBL:CCI32666.1, ECO:0000313|Proteomes:UP000004501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-4 {ECO:0000313|EMBL:CCI32666.1,
RC ECO:0000313|Proteomes:UP000004501};
RA Genoscope - CEA;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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:CCI32666.1}.
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DR EMBL; CAIP01000190; CCI32666.1; -; Genomic_DNA.
DR RefSeq; WP_008202142.1; NZ_CAIP01000190.1.
DR AlphaFoldDB; I4IEE2; -.
DR Proteomes; UP000004501; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03085; PGM1; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; 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 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:0000313|EMBL:CCI32666.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 14..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..287
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 296..408
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 59091 MW; 652D9E1BFD8385BE CRC64;
MTIETVATKP FSDQKPGTSG LRKSVPVFQQ PHYLENFIQA IFNTLDGIEG QTLVVGGDGR
YYNRQAIQTI LKIAAANGIG RILVGTDGIV STPAISGLIR ENNAFGGIVL SASHNPGGPE
GDFGIKYNIT NGGPAPENIT DAIYAETKVI SSYKILSGAD INLDRPSSFK LGTMDVEVID
AVTPYVKMME KIFDFDRIQA LLTSGKFKMC MDSLHAVTGP YAYALFEQRL GAPKGTVLNG
IPLEDFGGGH PDPNLVYAHD LVEILFGQDA PDFGAASDGD GDRNMILGRN FFVTPSDSLA
VLTANAHLVP GYQNGITGVA RSMPTSAAAD RVAAKLGIDC YETPTGWKFF GNLLDAGKAT
LCGEESFGTG SNHIREKDGL WAVLFWLNIL AVKGESVEEI VRSHWQEFGR NFYSRHDYEE
VALEPAKEMM ARLQKLVLDL KGKQFGNYEV EYADDFSYTD PVDGSVSKNQ GIRIGFTDGS
RIIYRLSGTG TKGATLRVYL ESYEPDASKH DIDTQKALQP LIDLAEEIGQ IRQSTGREQP
TVIT
//
