ID K0AAU4_EXIAB Unreviewed; 578 AA.
AC K0AAU4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 Name=pgcA {ECO:0000313|EMBL:AFS69796.1};
GN OrderedLocusNames=Eab7_0647 {ECO:0000313|EMBL:AFS69796.1};
OS Exiguobacterium antarcticum (strain B7).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1087448 {ECO:0000313|EMBL:AFS69796.1, ECO:0000313|Proteomes:UP000006274};
RN [1] {ECO:0000313|EMBL:AFS69796.1, ECO:0000313|Proteomes:UP000006274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|Proteomes:UP000006274};
RX PubMed=23144424; DOI=10.1128/JB.01791-12;
RA Carneiro A.R., Ramos R.T., Dall'Agnol H., Pinto A.C., de Castro Soares S.,
RA Santos A.R., Guimaraes L.C., Almeida S.S., Barauna R.A., das Gracas D.A.,
RA Franco L.C., Ali A., Hassan S.S., Nunes C.I., Barbosa M.S., Fiaux K.K.,
RA Aburjaile F.F., Barbosa E.G., Bakhtiar S.M., Vilela D., Nobrega F.,
RA Dos Santos A.L., Carepo M.S., Azevedo V., Schneider M.P., Pellizari V.H.,
RA Silva A.;
RT "Genome sequence of Exiguobacterium antarcticum B7, isolated from a biofilm
RT in Ginger Lake, King George Island, Antarctica.";
RL J. Bacteriol. 194:6689-6690(2012).
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; CP003063; AFS69796.1; -; Genomic_DNA.
DR RefSeq; WP_014969667.1; NC_018665.1.
DR AlphaFoldDB; K0AAU4; -.
DR STRING; 1087448.Eab7_0647; -.
DR KEGG; ean:Eab7_0647; -.
DR PATRIC; fig|1087448.3.peg.663; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_9; -.
DR Proteomes; UP000006274; 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}.
FT DOMAIN 43..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 326..452
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 520..559
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 578 AA; 63943 MW; FE3A2D022B8F25B9 CRC64;
MSWKETYQKW NQFSGLEAEL KQELTALAAD DKAAEDAFYK ELEFGTGGMR GEIGVGTNRM
NVYTVRKASQ GFADFIKAEG AEAVAQGIVI AHDSRHYSPE FALEAAKTLA SNGIKAYLFD
GLRPTPELSF AVRELRAAGG IVITASHNPP EYNGYKVYGN DGGQLPPKEA DDLVSYVDQV
ADELAIELEA EEVLRANGLI VRVGEQLDDA YQEQLKTIRV LPTIQDELTA PLKIVFTPLH
GTGLVPVTVG LKNYGFEHVT VVEEQAKPDG AFPTVSSPNP EEHAAFTLAI EYGNRVDADV
LLATDPDADR VGVATRDANG EWVVLTGNQT GALLLDYILS QKASQGTLPK NGFVAKTIVT
SELGTLIARH YDLHVENTLT GFKFIGEKIK QYNASGEYKY LFGYEESYGY LIGDFCRDKD
AVQACLLAAE MVAYHKKEGR TLYEALQAIY EQFGYFEESL RSLTLKGKDG VEQIGRIMDT
FREHPPKQVA GEKVVLFEDY DASIAHDLIQ HKPSPINLPK SNVLKFTLED GSWFCLRPSG
TEPKIKFYFS VTSPDAAETS RKRQMIEDEV MQEVEQIQ
//
