ID   A0A3N2KSK9_9BACT        Unreviewed;       582 AA.
AC   A0A3N2KSK9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:ROS88604.1};
GN   ORFNames=EEL39_05595 {ECO:0000313|EMBL:ROS88604.1};
OS   Muribaculaceae bacterium Isolate-080 (Janvier).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486468 {ECO:0000313|EMBL:ROS88604.1, ECO:0000313|Proteomes:UP000277934};
RN   [1] {ECO:0000313|EMBL:ROS88604.1, ECO:0000313|Proteomes:UP000277934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-080 (Janvier) {ECO:0000313|Proteomes:UP000277934};
RA   Clavel T., Strowig T.;
RT   "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT   host preference, and functional potential of this yet undescribed family.";
RL   Submitted (NOV-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:ROS88604.1}.
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DR   EMBL; RIBG01000004; ROS88604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2KSK9; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000277934; 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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
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};
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:UP000277934}.
FT   DOMAIN          51..189
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          213..321
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          327..452
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          508..554
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   582 AA;  64570 MW;  FDB01DA914B838B1 CRC64;
     MENEQLLKEV TAKAQVWLGD GYDEETRTEV KRMLDADDKT ELIESFYKDL EFGTGGLRGI
     MGAGTNRMNI YTVGAATQGL ANYLKENFKD LPEISVAVGH DVRNNSRKFA EIVADIFSAN
     GIKVYLFDSF RPTPELSFAI RHFGCQSGVN ITASHNPKIY NGYKAYWEDG AQIIAPHDVN
     IINHVNKIKR EDIKFDGDKS KIQIIGADVD KVYLEKIKGL SLSPDVIERH KDLKIVYTPI
     HGTGVELIPD SLRNFGFTNI IHVPEQDIPS GEFPTVESPN PEVPSAMAMA IAKAKEVNAD
     IVMASDPDAD RIGCVIRDNS GEYVLLNGNQ IVMILLNYII TRNKELGLLK GNEFAVKTIV
     TTETIKAICD AMNVRLFDCY TGFKWIAAVM RDNEDVLRYL GGGEESYGFL AETFVRDKDA
     VSACSLMAEA CAWAKDKGMD FQAMLADIYM KYGFSHEVGV SVVRPGKSGA EEIQALMKQF
     RENPPKSLAG SPVTVIKDYG SLDIIYTDGK PNEKLDFPCT SNVLQYFTED GSKVSVRPSG
     TEPKIKFYME VKVPMEKPED YDKCGKLAEA KVEALKKDLG IA
//