ID   B2KE73_ELUMP            Unreviewed;       518 AA.
AC   B2KE73;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain {ECO:0000313|EMBL:ACC98819.1};
GN   OrderedLocusNames=Emin_1269 {ECO:0000313|EMBL:ACC98819.1};
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC98819.1, ECO:0000313|Proteomes:UP000001029};
RN   [1] {ECO:0000313|EMBL:ACC98819.1, ECO:0000313|Proteomes:UP000001029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191 {ECO:0000313|EMBL:ACC98819.1,
RC   ECO:0000313|Proteomes:UP000001029};
RX   PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
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}.
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; CP001055; ACC98819.1; -; Genomic_DNA.
DR   RefSeq; WP_012415434.1; NC_010644.1.
DR   AlphaFoldDB; B2KE73; -.
DR   STRING; 445932.Emin_1269; -.
DR   KEGG; emi:Emin_1269; -.
DR   HOGENOM; CLU_016950_7_1_0; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000001029; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001029}.
FT   DOMAIN          33..162
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          194..304
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          308..421
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          436..508
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   518 AA;  56438 MW;  5BDD1636232EC5B9 CRC64;
     MADINAGKLP VKTIDMELLK KEFFNPSGSL AKVKFGTSGH RGELGKGFCA LHAKAIAQAV
     AKMHKEDGIK GPVLVGGDTR LMSKTVSEIC ACILAANGID VILPSIPLPT PVFSMEILLG
     RACACLNGTA SHNPPQDMGL KYNPSNGGPA DSSVTSKIEE YANYFMATPS EIKEIGLEEA
     KQSGLIKEED VITPYITELA KVIDFDAIKE KGLKAAIHPM GGTSLPFYKA IKEKYKLDNL
     TIVNETIDPT FYFIPLDHDG KTRMDPSSQY PMKPLIDIVA AGEYDFAGAS DPDADRFGCA
     TKEGGLINPN HALCVMAEYL ISKNKSNFDK YIGRTLGTTH LLDFIAKSAG VEIDEQNVGF
     KYFVQGIKDG KYILCGEESA GMSKSGWTTE KDGIFAVLLL LEIMSKNADI AYLYKEITKK
     YGVSYYTRVD IPTDDETKAK VKSLKATDVA SVTEVAGEKV EKVRDTDGIK IYLQNSWFLV
     RPSGTENIIK FYCESFISEE QMLKIVKEGS AALGIKLS
//