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Database: UniProt
Entry: A0A0F8AYB7_9EURY
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ID   A0A0F8AYB7_9EURY        Unreviewed;       466 AA.
AC   A0A0F8AYB7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KKF39755.1};
GN   ORFNames=FK85_26055 {ECO:0000313|EMBL:KKF39755.1};
OS   Halorubrum saccharovorum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=2248 {ECO:0000313|EMBL:KKF39755.1, ECO:0000313|Proteomes:UP000053331};
RN   [1] {ECO:0000313|EMBL:KKF39755.1, ECO:0000313|Proteomes:UP000053331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|EMBL:KKF39755.1,
RC   ECO:0000313|Proteomes:UP000053331};
RA   Rozanov A.S., Kotenko A.V., Bryanskaya A.V., Malup T.K., Peltek S.E.;
RT   "Full genome sequence of Halorubrum H3 strain isolated from Burlinskoye
RT   Salt Lake (Altai Krai, Russia).";
RL   Submitted (MAR-2015) 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}.
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:KKF39755.1}.
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DR   EMBL; JNFH02000020; KKF39755.1; -; Genomic_DNA.
DR   RefSeq; WP_050024425.1; NZ_JNFH02000020.1.
DR   AlphaFoldDB; A0A0F8AYB7; -.
DR   OrthoDB; 10363at2157; -.
DR   Proteomes; UP000053331; Unassembled WGS sequence.
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   CDD; cd05800; PGM_like2; 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; 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.
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:UP000053331}.
FT   DOMAIN          5..134
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          175..258
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          269..359
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          401..462
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   466 AA;  49263 MW;  19EF26E09725C1D8 CRC64;
     MDEIAFGTDG WRATLDTFTD ERVRIVGQAV ADHLAAAGHD EPVAVGYDAR ETSEGFAESL
     AEVLAGNGFD VLLPERDAPT PVIAYAIVDR GLAGACMVTA SHNPPEYNGV KFIPDDGAPA
     LPDVTEDIVD RLAEPDLLPE AERGEVSRVD LVSDHADAAR EVVGAATGGK GVDLDGLTVA
     YDAMHGSGRG VTDALLESAG AEVVRLRCER DVTFGGGSPE PSAEHLEALA ARVTDPDSDV
     DLGIANDGDA DRIAVVTPER GVLNANLFYA ACYDRLLEND SGPAVRTVST TFLVDRIAEA
     HGEDVYETPV GFKWVAEAMG ERDALFGGEE SGGFTLRSHV REKDGVLMAL LAAGTHAAEP
     FDDRVDRLLD EHGAIASGRV SLDCPDARKE AVLDDLEDHI PESVAGHGVA KVVTLDGFKL
     LLENGSWLLV RPSGTEPKLR VYAEADSEAA VDDLLAEGRE IVEPLI
//
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