ID G6AET0_9BACT Unreviewed; 581 AA.
AC G6AET0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9138_00607 {ECO:0000313|EMBL:EHG16777.1};
OS Prevotella histicola F0411.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=857291 {ECO:0000313|EMBL:EHG16777.1, ECO:0000313|Proteomes:UP000004597};
RN [1] {ECO:0000313|EMBL:EHG16777.1, ECO:0000313|Proteomes:UP000004597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0411 {ECO:0000313|EMBL:EHG16777.1,
RC ECO:0000313|Proteomes:UP000004597};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Mathney J.M.J., Dewhirst F.E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella histicola F0411.";
RL Submitted (OCT-2011) 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:EHG16777.1}.
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DR EMBL; AFXP01000004; EHG16777.1; -; Genomic_DNA.
DR RefSeq; WP_008822523.1; NZ_JH376762.1.
DR AlphaFoldDB; G6AET0; -.
DR STRING; 857291.HMPREF9138_00607; -.
DR GeneID; 66730919; -.
DR PATRIC; fig|857291.3.peg.593; -.
DR HOGENOM; CLU_016950_0_0_10; -.
DR Proteomes; UP000004597; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004597}.
FT DOMAIN 52..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..319
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 581 AA; 65321 MW; 9A63CE73B63DD97B CRC64;
MENNQALIAQ CESKAKQWLS PAFDEETRSA VNRMIANEDK TDLIESFYKD LEFGTGGLRG
IMGAGSNRMN IYTVGMATQG FANYLKINFK DKKQISVVVC HDCRNNSRLF AETVANIFSA
NGIKVYLFED LRPTPECSFA IRYLKAQAGV NITASHNPRE YNGYKAYWED GAQVLAPHDK
GIIDEVNKVK IEDVKFEGNK ALIQSIGEDI DKPYLDRVKT VSIDPEVIKH QHDLKIVYTP
LHGAGRVMIP RSLALWGFDN VHCVKEQMVK DGNFPTVDRP NPEIAEALTL GLRDAKALDA
DILMASDPDA DRVGMACKDS NGEWVLINGN QTCLIFLWYI ITNRQAVGKM KPTDFIVKTI
VTTEVIRKIA EKQHVEMRDC YTGFKWIARE IAISEGKQQY IGGGEESYGF LAEDFVRDKD
AVSACSLLAE ICAYAKDHGK TLYDILMDIY LEYGYSHEHT INVERPGKSG ADEIQQMMKD
FRTNPPKDLG GSPISIYKDY QSLEMTKVDG SNEKIDMPDT SNVLQWFCSD GTKVSVRPSG
TEPKIKFYLE IKDKMCSASD YPACEQRAVT KIEEIKKSLK L
//
