ID   A0A1H3Z9E8_9EURY        Unreviewed;       451 AA.
AC   A0A1H3Z9E8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Phosphomannomutase / phosphoglucomutase {ECO:0000313|EMBL:SEA20413.1};
GN   ORFNames=SAMN04488065_2239 {ECO:0000313|EMBL:SEA20413.1};
OS   Haloplanus vescus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloplanus.
OX   NCBI_TaxID=555874 {ECO:0000313|EMBL:SEA20413.1, ECO:0000313|Proteomes:UP000236755};
RN   [1] {ECO:0000313|EMBL:SEA20413.1, ECO:0000313|Proteomes:UP000236755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8712 {ECO:0000313|EMBL:SEA20413.1,
RC   ECO:0000313|Proteomes:UP000236755};
RA   de Groot N.N.;
RL   Submitted (OCT-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   ---------------------------------------------------------------------------
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; FNQT01000003; SEA20413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3Z9E8; -.
DR   STRING; 555874.SAMN04488065_2239; -.
DR   OrthoDB; 10363at2157; -.
DR   Proteomes; UP000236755; 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   CDD; cd03087; PGM_like1; 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   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:UP000236755}.
FT   DOMAIN          2..130
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          150..250
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          255..362
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          395..448
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   451 AA;  47169 MW;  0973A68AF623E1F4 CRC64;
     MELFGSSGTR GVVGETFTPT LVRDVSAAAA AVWDADRVAV ARDTRDSGEA FTDVAAGTLT
     AAGADVDRLG ILPTPAVSYY CEREGVPAVH ITASHNPPEY NGIKLLGADG TELSVDGYGR
     VEDRIFAETE SLAAWDAVGT SRPVDGVAAD YRADMRAGVD TDAIADADLT VAIDPGHGAG
     SAVSPDFVRE LGCAVRTVNA DPDGRFPGRD PEPVPENLGA LRRLVRSTDA DVGVAHDGDA
     DRAIFVDETG AMIDGDTSFA ALAAAELAAG DTVVAAVNVS QRVVDAVDAA GASLELTPIG
     AAHIVTRVRK CREAGQKVPI AGEGNGGVFF PGHRLTRDGP YIAAKFLERL AAADAPASEV
     VAPYAGYHLV RDAVEYDGDA ERDRLLDAAE AYAREADADL NTTDGYRLDY GDAWVLVRPS
     GTEPKVRIYA EAREKERAAT LVDDVHAHLT D
//