ID   A0A3E0IAU6_9PSEU        Unreviewed;       549 AA.
AC   A0A3E0IAU6;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:REH55721.1};
GN   ORFNames=BCF44_101747 {ECO:0000313|EMBL:REH55721.1};
OS   Kutzneria buriramensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1045776 {ECO:0000313|EMBL:REH55721.1, ECO:0000313|Proteomes:UP000256269};
RN   [1] {ECO:0000313|EMBL:REH55721.1, ECO:0000313|Proteomes:UP000256269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45791 {ECO:0000313|EMBL:REH55721.1,
RC   ECO:0000313|Proteomes:UP000256269};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (AUG-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:REH55721.1}.
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DR   EMBL; QUNO01000001; REH55721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0IAU6; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000256269; 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   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   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}.
FT   DOMAIN          54..188
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          223..308
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          322..433
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          470..515
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   549 AA;  57195 MW;  06AFB315B5F5D094 CRC64;
     MSIAPALRDA TFRWIADDPD QDARTELQGI LAQAIAGDQA SIDELADRMG GPLTFGTAGL
     RGPVRAGANG MNEAVVVRTT AGLADWLQRN GHGGGVVVVG RDARHGSEQF HRAAAGVLAA
     AGFDVRVLDG PLPTPVTAFL VRRLNAVAGV QITASHNPPA DNGYKLYIEH GAQIVPPTDR
     QIEAAIAQVP AAVSVPRSTN WTTVSADDVA AYVTRAASLP VGGVRTLRVA ATPMHGVGAA
     TLASVLAAAE FTDVHFVPQQ QDPDADFPTV SFPNPEEPGA TDLLLALAES VDADLAIALD
     PDADRCALGV RERDGSWRML RGDETGVLLG EHVLSTMDAT GALVATTIVS SSLLSKVAAA
     HGARYDETLT GFKWLVRAGD GAGTGLVYAY EEALGHCVDP DYVRDKDGIS AAVLACDLAA
     GLKAEGRTPL DVLDDLAVAH GLHLTDQVSL RVTDLGRIGV LMAKLRTEPP AALAGVSVAA
     EDLRPRADVL ALRGEGVRVL IRPSGTEPKL KAYLEIVEPV PDRDGLAAAR QRAVARLAAL
     RGDVAALFE
//