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Database: UniProt
Entry: A0A239QUP6_9MICO
LinkDB: A0A239QUP6_9MICO
Original site: A0A239QUP6_9MICO 
ID   A0A239QUP6_9MICO        Unreviewed;       230 AA.
AC   A0A239QUP6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I {ECO:0000313|EMBL:SNU01875.1};
GN   ORFNames=SAMN06298212_11914 {ECO:0000313|EMBL:SNU01875.1};
OS   Ruaniaceae bacterium KH17.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae.
OX   NCBI_TaxID=1945888 {ECO:0000313|EMBL:SNU01875.1, ECO:0000313|Proteomes:UP000214750};
RN   [1] {ECO:0000313|EMBL:SNU01875.1, ECO:0000313|Proteomes:UP000214750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH17 {ECO:0000313|EMBL:SNU01875.1,
RC   ECO:0000313|Proteomes:UP000214750};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; FZQV01000019; SNU01875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239QUP6; -.
DR   Proteomes; UP000214750; 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   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 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; 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   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000214750}.
FT   DOMAIN          3..134
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   REGION          187..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  25326 MW;  0B75BF40F473A395 CRC64;
     MIHFGTGGWR EIIGDQFTRE NVRRITQALC NRMSAEGVTE RGIVVGYDRR FLSGEAALWA
     TEVFLGNGVP VTLIDRFAPT PMIMWTVRDK NCAYGLAVTA SHNPALYNGL KIFTEGGRDA
     ELAVTDEIAA AANALTVDDV VGIESYEVDA SPLLTKQSSI NWYIDAIIEK LDMDTIRHGH
     LHVADRSDVR RGADQHADHP DDGALPGGRN QRPPRHPVWR PAPLPLRGHA
//
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