ID A0A0B0DAE7_9BACI Unreviewed; 169 AA.
AC A0A0B0DAE7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE Flags: Fragment;
GN ORFNames=LD39_01040 {ECO:0000313|EMBL:KHE73117.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE73117.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE73117.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE73117.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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:KHE73117.1}.
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; JRNX01000021; KHE73117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0DAE7; -.
DR Proteomes; UP000030879; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase 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; 1.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030879}.
FT DOMAIN 83..144
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KHE73117.1"
SQ SEQUENCE 169 AA; 19007 MW; A67739C3415E175B CRC64;
YLVKDFARDK DAVQAAVLIA EVGAYYKNQG KTLLDALDEL YQKHGYFLED LLSVKLDGKS
GADKIKEIMD DFREADIKEV GGKKVVAIED YATTVRHYVE GGTTEEIDLP TSNVLKFILE
DDCWFCLRPS GTEPKIKFYF GVKTSSMSDS QNLLESLKST VNQRLHALI
//