ID A0A5W4L432_SALEN Unreviewed; 477 AA. AC A0A5W4L432; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 29-SEP-2021, entry version 5. DE SubName: Full=Alpha-D-glucose phosphate-specific phosphoglucomutase {ECO:0000313|EMBL:EBW8917198.1}; DE Flags: Fragment; GN ORFNames=BXJ37_24110 {ECO:0000313|EMBL:EBW8917198.1}; OS Salmonella enteritidis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=149539 {ECO:0000313|EMBL:EBW8917198.1, ECO:0000313|Proteomes:UP000327671}; RN [1] {ECO:0000313|EMBL:EBW8917198.1, ECO:0000313|Proteomes:UP000327671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=299857 {ECO:0000313|EMBL:EBW8917198.1, RC ECO:0000313|Proteomes:UP000327671}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (AUG-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:EBW8917198.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHJOO010000030; EBW8917198.1; -; Genomic_DNA. DR Proteomes; UP000327671; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. 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; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005852; PGlcMutase_a-D-Glc-sp. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR SUPFAM; SSF53738; SSF53738; 3. DR TIGRFAMs; TIGR01132; pgm; 1. 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}. FT DOMAIN 40..179 FT /note="PGM_PMM_I" FT /evidence="ECO:0000259|Pfam:PF02878" FT DOMAIN 210..317 FT /note="PGM_PMM_II" FT /evidence="ECO:0000259|Pfam:PF02879" FT DOMAIN 320..440 FT /note="PGM_PMM_III" FT /evidence="ECO:0000259|Pfam:PF02880" FT NON_TER 477 FT /evidence="ECO:0000313|EMBL:EBW8917198.1" SQ SEQUENCE 477 AA; 50690 MW; 8D35DB0D2ACF1302 CRC64; MAIHNRAGQP AQQSDLINVA QLTAQYYVLK PEAGNAEHAV KFGTSGHRGS AGRHSFNEPH ILAIAQAIAE ERAKNGITGP CYVGKDTHAL SEPAFISVLE VLAANGVDVI VQENNGFTPT PAVSNAILVH NKKGGPLADG IVITPSHNPP EDGGIKYNPP NGGPADTNVT KVVEDRANAL LAGGLQGVKR ISLDAAMASG HVKAVDLVQP FVEGLADIVD IAAIQKAGLT LGVDPLGGSG IEYWKRIAEH YKLNLTLVND QVDQTFRFMH LDKDGAIRMD CSSECAMAGL LALRDKFDLA FANDPDYDRH GIVTPAGLMN PNHYLAVAIN YLFQHRPLWG KDVAVGKTLV SSAMIDRVVN DLGRKLVEVP VGFKWFVDGL FDGSFGFGGE ESAGASFLRF DGTPWSTDKD GIIMCLLAAE ITAVTGKNPQ EHYNELAKRF GAPSYNRLQA AATSAQKAAL SKLSPEMVSA STLAGDP //