ID V9GME0_9BACL Unreviewed; 572 AA.
AC V9GME0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN ORFNames=JCM10914_6226 {ECO:0000313|EMBL:GAE09834.1};
OS Paenibacillus sp. JCM 10914.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE09834.1, ECO:0000313|Proteomes:UP000018028};
RN [1] {ECO:0000313|EMBL:GAE09834.1, ECO:0000313|Proteomes:UP000018028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE09834.1,
RC ECO:0000313|Proteomes:UP000018028};
RA Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA Hattori M.;
RT "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL Genome Announc. 2:e01144-13(2014).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005164}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:GAE09834.1}.
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; BAUO01000048; GAE09834.1; -; Genomic_DNA.
DR RefSeq; WP_023967070.1; NZ_BAZR01000048.1.
DR AlphaFoldDB; V9GME0; -.
DR STRING; 1236974.GCA_001315105_06108; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000018028; 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:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
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:UP000018028}.
FT DOMAIN 48..187
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 232..322
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 334..460
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 502..545
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 572 AA; 62906 MW; 14FC04AACA06F5EB CRC64;
MSEISQRTMD TVQRWLNDPL VDEETKQELR DLQQDEAELE ERFYRDLEFG TGGLRGVIGA
GSNRINKYTV GRATQGFAQY ILQAHGKAEG TPSVVIAHDS RHFSPEFALE AALVLAGNGI
TAKLYPSLRS TPQLSFSVRH LGATGGIVIT ASHNPPEYNG YKVYNAEGGQ LVPDEAEQVI
ALIQQVDSFA SVKRLSQEEA EAQALLVWLG EADDQAFVDT VMDISLNRDS IASHLGEDFR
IVFTPLHGTG GEPVRRALEG IGFRHIHVVQ EQAQPDGDFP TVKSPNPEER EAFTLAMKLG
EEVGADILIG TDPDADRMGA VVKNSQGEYV VLTGNQSGAI MIHYVLGRLK EAGKLPDNGA
VIKTIVTSEM GAVIAEHYGA KVFNTLTGFK YIGEKMTQFE ESGSHTYLFG YEESYGYLAG
HYARDKDAVL ASMLICESAA YYKGQGKTLY DVLQELYEEF GYFLETLQSR TLKGKDGVAQ
IQAKMSNWRD QPPTQIGGVA VQQVLDYAEG LDGLPKENVL KYMLEDGSWF CLRPSGTEPK
IKVYFAVRGH SFDDAQHKMA ALSDHVMARV DA
//