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Database: UniProt
Entry: U2L6S5_9BACT
LinkDB: U2L6S5_9BACT
Original site: U2L6S5_9BACT 
ID   U2L6S5_9BACT            Unreviewed;       582 AA.
AC   U2L6S5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Putative phosphoglucomutase {ECO:0000313|EMBL:ERK00208.1};
GN   ORFNames=HMPREF1218_1280 {ECO:0000313|EMBL:ERK00208.1};
OS   Hoylesella pleuritidis F0068.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=1081904 {ECO:0000313|EMBL:ERK00208.1, ECO:0000313|Proteomes:UP000016600};
RN   [1] {ECO:0000313|EMBL:ERK00208.1, ECO:0000313|Proteomes:UP000016600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0068 {ECO:0000313|EMBL:ERK00208.1,
RC   ECO:0000313|Proteomes:UP000016600};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERK00208.1}.
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DR   EMBL; AWET01000038; ERK00208.1; -; Genomic_DNA.
DR   RefSeq; WP_021584287.1; NZ_AWET01000038.1.
DR   AlphaFoldDB; U2L6S5; -.
DR   PATRIC; fig|1081904.3.peg.1672; -.
DR   Proteomes; UP000016600; 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:UP000016600}.
FT   DOMAIN          52..189
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          214..318
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   582 AA;  65842 MW;  13346FC03536EEA0 CRC64;
     MENNVELIAQ CEKKAKQWLA PAFDAETRRE VQAMLDNSDK TDLIESFYKE LEFGTGGLRG
     IMGAGSNRMN IYTVGMATQG FANYLKKNFA NRADISVVVC HDCRNNSRLF AETVADIFSA
     NGIKAYIFDD MRPTPECSFA IRHLHCQAGV NITASHNPKE YNGYKAYWED GAQVLTPHDT
     GIIDEVNKVK VEDVKFDRNK ELIETIGEEI DKIYLEQIRT LSIDPEVIKR QKDLKIVYTP
     LHGTGMMLIP RSLQLWGFEN VYCVKEQMER SGDFPTVVSP NPENSETLTL ALRDAKALDA
     DIVMASDPDA DRVGMACKND KGEWILINGN QTCLIFLYYI ITNRIKMGKM KPTDFIVKTI
     VTTEVIRKIA EKQHIEMRDC YTGFKWIARE IALSEGKQKY IGGGEESYGF LAEDFVRDKD
     SVSACSLLAE ICAYAKDQGK TLYDLLMDIY LEYGFSKEFT INVVRPGKSG ADEIKQMMEN
     FRKNPPTDLG GSKVVVWKDY QSLKQRDEQG NVTPIDMPAT SNVLQWFCND DTKVSVRPSG
     TEPKIKFYLE VKGTMKCPGC YERCDKEGAE KVEAIKKSLH LD
//
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