ID A0A011P6I2_9PROT Unreviewed; 547 AA.
AC A0A011P6I2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
GN Name=pgm {ECO:0000313|EMBL:EXI72510.1};
GN ORFNames=AW07_03239 {ECO:0000313|EMBL:EXI72510.1};
OS Candidatus Accumulibacter sp. SK-11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI72510.1, ECO:0000313|Proteomes:UP000020226};
RN [1] {ECO:0000313|EMBL:EXI72510.1, ECO:0000313|Proteomes:UP000020226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-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 -!- 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:EXI72510.1}.
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DR EMBL; JFAW01000022; EXI72510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011P6I2; -.
DR STRING; 1454000.AW07_03239; -.
DR PATRIC; fig|1454000.3.peg.2696; -.
DR Proteomes; UP000020226; Unassembled WGS sequence.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 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:0000313|EMBL:EXI72510.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000020226}.
FT DOMAIN 16..155
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 186..290
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 299..411
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 547 AA; 58307 MW; 0FFE80C06EA9FBE5 CRC64;
MTMQVISVPS TPFAGQKPGT SGLRKKVKVF SQARYLENFV QAIFDTLSGQ QGQTLVLGGD
GRYYNDVAIQ TILRMAAAAG FGRVLVGCDG ILSTPAASAV IRKWQAFGGI ILSASHNEGG
PEGDFGIKYN LGNGGPANEA FTDAVYRRTQ EISAYRTVDS PAVDLSRLGE SHIGDMRVSV
IDPVADYAEL LESLFDFDRI AALLARPDFR MRFDAMHAVT GPYARAILET RLGAPAGTVV
NGIPLPDFAG GHPDPNPVWA ADLVSALADP ASGLSFGAAS DGDGDRNMIV GPDFVVSPSD
SLAVLAANHA LVPAYAGGLA GVARSMPTSC AVDRVARALG IPCYETPTGW KYFGSLLDAG
KATLCGEESA GTGSNHVREK DGLWAVLYWL NILAVRATSA DVIVREHWRR FGRNVYSRHD
YEAIETALAD RLMDELRARL PQLAGSESCG LRIAAADDFS YTDPVDGSRS ERQGVRVMLD
DGSRVVFRLS GTGTEGATLR VYLERFVADP SQHEVPTQEA LAPLIRLADA VAQITAITGR
RKADVIS
//
