ID A0A443IAS2_9GAMM Unreviewed; 546 AA.
AC A0A443IAS2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:RWR01115.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:RWR01115.1};
GN ORFNames=ED28_15165 {ECO:0000313|EMBL:RWR01115.1};
OS [Pantoea] beijingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1324864 {ECO:0000313|EMBL:RWR01115.1, ECO:0000313|Proteomes:UP000288794};
RN [1] {ECO:0000313|EMBL:RWR01115.1, ECO:0000313|Proteomes:UP000288794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27579 {ECO:0000313|EMBL:RWR01115.1,
RC ECO:0000313|Proteomes:UP000288794};
RA Xu F., Liu Y., Wang S., Yin Y., Ma Y., Zhao S., Rong C.;
RT "Draft genome sequence of Pantoea beijingensis strain LMG 27579, an
RT emerging pathogen to Pleurotus eryngii with potential industrial
RT application.";
RL Submitted (APR-2014) 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:RWR01115.1}.
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DR EMBL; JMEE01000040; RWR01115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443IAS2; -.
DR Proteomes; UP000288794; 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; 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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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 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, ECO:0000313|EMBL:RWR01115.1};
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:UP000288794}.
FT DOMAIN 40..178
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 320..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 489..539
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 546 AA; 58583 MW; 1FB6AE2F4BCA8874 CRC64;
MANHPRAGQP ARQSDLINVA QLTSQYYVLQ PDVANTEHAV KFGTSGHRGS AGRHSFNEPH
ILAIAQAIAE ERKKNGITGP CFVGKDTHAL SEPAMISVLE VLAANGVDVI VQQDNGYTPT
PAISNAILEH NKSGSTLADG IVITPSHNPP EDGGIKYNPP NGGPADTNVT KVVEDRANAL
IGDGLKEVKR LSLDLAWASG HIQEKDLIQP YIEGLAQVVD IPAIQKAGLK IGVDPLGGSG
IAYWQRIAEF YQLDLTLVND AVDQTFRFMH LDKDGVVRMD CSSESAMAGL LALRDKFDLA
FGNDPDYDRH GIVTPAGLMN PNHYLAVAIN YLFQHRPQWG KEVAVGKTLV SSAMIDRVVN
DIGRTLVEVP VGFKWFVDGL FDGSFGFGGE ESAGASFLRF DGTPWSTDKD GIIMCLLAAE
ITAVTGKNPQ QHYDELAERF GAPSYNRLQA PATSAQKAAL SKLSPEMVSA DTLAGDAITA
RLTAAPGNGA SIGGLKVMTE NGWFAARPSG TEDAYKIYCE SFLGAEHREK IEKEAVEIVS
EVLKNV
//
