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Database: UniProt
Entry: A0A0D3VFF6_9BACL
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ID   A0A0D3VFF6_9BACL        Unreviewed;       572 AA.
AC   A0A0D3VFF6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=UB51_20240 {ECO:0000313|EMBL:AJS60392.1};
OS   Paenibacillus sp. IHBB 10380.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS60392.1, ECO:0000313|Proteomes:UP000032320};
RN   [1] {ECO:0000313|EMBL:AJS60392.1, ECO:0000313|Proteomes:UP000032320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS60392.1,
RC   ECO:0000313|Proteomes:UP000032320};
RX   PubMed=25908145;
RA   Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using
RT   PacBio Single-Molecule Real-Time Sequencing Technology.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP010976; AJS60392.1; -; Genomic_DNA.
DR   RefSeq; WP_044878836.1; NZ_CP010976.1.
DR   AlphaFoldDB; A0A0D3VFF6; -.
DR   STRING; 1566358.UB51_20240; -.
DR   KEGG; pih:UB51_20240; -.
DR   PATRIC; fig|1566358.3.peg.4422; -.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000032320; Chromosome.
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:UP000032320}.
FT   DOMAIN          48..186
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          223..323
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          509..551
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   572 AA;  63377 MW;  66D32CB46DA184F5 CRC64;
     MTVLSQQSKD QIQEWLQDKH IDEATKQELR DLENEPNELE DRFYKDLEFG TGGLRGIIGA
     GSNRINRYTV GKATQGFAQY ILAKHGESEG KPSVVIAHDS RHYSPEFALE AALVLAGNGI
     VAKLFPSLRT TPQLSFSVRH LGATGGIVVT ASHNPPEYNG YKVYNDQGGQ LIPHEAEQVI
     KYIQEVEAFA AVKRLDQATA EAEGLLVWLG EADDEAFVHT VAQTSVNAEL IRSTLGQDFT
     IVYTPLHGTG NLPVRRVLES VGFTNVHVVP EQEQPDAEFS TVKSPNPEER EAFTLAIELG
     QRIDADILIG TDPDCDRMGA VVKNKLGEYE VLSGNQSGAI MIHYLLSQLK EAGQLPDNGL
     VIKTIVTSEM GATIAKYYGA EVINTLTGFK YIGEKMTQYE QSGEYTYLFG YEESYGYLAG
     NYARDKDAVL ASLLIAEAGA YYKAQGKTLY DVLQELYEQF GYFQESLESR TLMGKDGVAQ
     IQAKMTDWRS NPPQEIVGVR MQQVLDYSLG LEGLLKENVL KFMLEDGSWF CLRPSGTEPK
     IKVYFAVRGE SIMDAQQRIT SLAREVMARV DA
//
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