ID A0A2V3PP58_9BACT Unreviewed; 582 AA.
AC A0A2V3PP58;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:PXV64483.1};
GN ORFNames=CLV62_110127 {ECO:0000313|EMBL:PXV64483.1};
OS Dysgonomonas alginatilytica.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=1605892 {ECO:0000313|EMBL:PXV64483.1, ECO:0000313|Proteomes:UP000247973};
RN [1] {ECO:0000313|EMBL:PXV64483.1, ECO:0000313|Proteomes:UP000247973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100214 {ECO:0000313|EMBL:PXV64483.1,
RC ECO:0000313|Proteomes:UP000247973};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PXV64483.1}.
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DR EMBL; QICL01000010; PXV64483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3PP58; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000247973; Unassembled WGS sequence.
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; 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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 51..190
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..453
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 582 AA; 64507 MW; F59A2B95CF7B6E0E CRC64;
MENKELLKQV TSKANVWLAG DYDAETKADV QRMLNNTDKT DLMESFYKDL EFGTGGLRGI
MGVGTNRINK YTLGAATQGL SNYLLKQFSH LEQIKVVIGY DCRNNSKYFG QVVADIFSAN
GIKVYLFENL RPTPEVSFAI RTLGCQSGVI LTASHNPKEY NGYKAYWDDG AQVTPPHDKN
IIEEVNSISS VAEIKFTGNP ALIESLGEDM DNKFIESLKA ILLSPESIKR HGNIGIVYTP
IHGTGGQIVP QALKAYGFTN IIHVPEQDVV DGNFPTVVSP NPEEPAAMAM AVKKGIETGA
DLVFATDPDA DRFGAGVRDT NGDFILLNGN QTMIILIYYL VTRWKELGKL TGTEYTVRTI
VTSELTQVIS EKNGVEMFEC FTGFKWIASV MRQLEGKRQY IGGGEESYGF LAEDFVRDKD
SVSSAALFAE IAAWCKDNGR TIYEMLQDIY VEYGFSKEKG ISVVKKGMSG AQEIQSMMDN
FRNNPLEEIA GSKVTLVKDF EILEVKDLIT GKISKLDMPA TSNVLQYFTE DKTKVSIRPS
GTEPKIKFYI EVVDKLPSRA DFEKVDAATE AKIEQICKDL GI
//
