ID A0A0G0PRH8_9BACT Unreviewed; 494 AA.
AC A0A0G0PRH8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KKR30538.1};
GN ORFNames=UT61_C0005G0019 {ECO:0000313|EMBL:KKR30538.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA1_39_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618552 {ECO:0000313|EMBL:KKR30538.1, ECO:0000313|Proteomes:UP000034793};
RN [1] {ECO:0000313|EMBL:KKR30538.1, ECO:0000313|Proteomes:UP000034793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR30538.1}.
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DR EMBL; LBXL01000005; KKR30538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0PRH8; -.
DR Proteomes; UP000034793; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 34..157
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 178..271
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 277..384
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 392..463
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 494 AA; 55794 MW; E24EB47EF135FB4F CRC64;
MQVNPSIFRE YDIRGIAGEE FSDKALQEYE KWYGKFPGIT ITPDVAIVLG KAYGTQIRKR
GGKNIIIGHE ERQYGDELKR LFIDGMRSTG CDITDAGVSL TPIIYFSTAF YKFDGGVNVT
GSHNIYFFNG FKMMAKDVYP VYGEEIQEMK NIIEKDDYHL DIQGNLTQKN VFDDYKKYLL
DHNKLNKKMK IVLDCGNGSA GLFAPNLLRE LGCEVIEMYS EVDATFPNHV PDPEDKFVMQ
ELAGRVVQVK ADLGIGLDAD GDRFGCVDEK GEFIYADRMM LILAKDILSR NPGKKILYDV
KCTKLMEELV PKYGGVPYMH VTGHAPIKAT LRNDLEVIFA GEISGHFYWV EDYFKIDDGV
YSAAKILSFI SGQDKKLSEI MSEVPVTSMT PEIKLPCADE VKVKVANDIK EKFEKTYKVI
TIDGARVVFS DTSWALVRPS NTSPYLTIRV EADTDEEVIK IKNIMQDEFD KYPEIGDKLD
RGNVTSHTGK LGWV
//
