ID   A0A133PSY1_9BACT        Unreviewed;       475 AA.
AC   A0A133PSY1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KXA31953.1};
GN   ORFNames=HMPREF3226_02804 {ECO:0000313|EMBL:KXA31953.1};
OS   Prevotella corporis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA31953.1, ECO:0000313|Proteomes:UP000070533};
RN   [1] {ECO:0000313|Proteomes:UP000070533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJR7716 {ECO:0000313|Proteomes:UP000070533};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2016) 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:KXA31953.1}.
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DR   EMBL; LRQG01000263; KXA31953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133PSY1; -.
DR   STRING; 28128.HMPREF3226_02804; -.
DR   PATRIC; fig|28128.5.peg.2889; -.
DR   eggNOG; COG1109; Bacteria.
DR   Proteomes; UP000070533; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; 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; 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   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR024086; GlmM_arc-type.
DR   NCBIfam; TIGR03990; Arch_GlmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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   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   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:UP000070533}.
FT   DOMAIN          20..154
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          183..275
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          282..385
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          408..467
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   475 AA;  52026 MW;  8429FDEB6C2789AC CRC64;
     MEAIKRYKEN NTMTLIKSIS GIRGTIGGHT GDTLNPLDIV KFTSAYATFI ASKHPDKKLK
     IVVGRDARIS GEMVKNIVCG TLMGIGADVV NIGLATTPTT ELAVRMSGAD GGIIITASHN
     PRQWNALKLL NHEGEFLTAS EGAEVLNIAE REDFNYADVD KLGQYTEDNT YNQKHIEAVK
     ALKLADLTAI RERKFRVCVD TINSVGGVIL PKLLDELGVE YKILYGEPTG DFAHNPEPIE
     KNLSGIMEEM RKGGYDLGIV VDPDVDRLAF IQEDGVMFGE EYTLVSVADY ILDHVKGNTV
     SNLSSTRALR DVTEKHGGKY YASAVGEVNV TTKMKEVNAV IGGEGNGGVI YPESHYGRDA
     LVGIVLFLSS LAQKGLKASE LRKTYPSYFI AKNRIDLTPE TNVDAILAKV KELYGQESDV
     QVTDIDGVKL DFPTSWVHLR KSNTEPIIRI YSEAGSMKEA DALGKKLMQV VYDMQ
//