ID A0A0G1SWW6_9BACT Unreviewed; 486 AA.
AC A0A0G1SWW6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KKU74024.1};
GN ORFNames=UX98_C0002G0054 {ECO:0000313|EMBL:KKU74024.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_26.
OC Bacteria.
OX NCBI_TaxID=1618844 {ECO:0000313|EMBL:KKU74024.1, ECO:0000313|Proteomes:UP000034356};
RN [1] {ECO:0000313|EMBL:KKU74024.1, ECO:0000313|Proteomes:UP000034356}
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:KKU74024.1}.
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DR EMBL; LCOG01000002; KKU74024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1SWW6; -.
DR STRING; 1618844.UX98_C0002G0054; -.
DR PATRIC; fig|1618844.3.peg.157; -.
DR Proteomes; UP000034356; 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 30..163
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 177..275
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 281..388
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 395..474
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 486 AA; 54005 MW; 9E22D34BFF6F1EAC CRC64;
MIVVKFMHIL YNNIPNKRNH NFNMRLEPTM FRKYDIRGRV SDAEFNEKSV EAIAKGFGTM
LRKRGVETCV CAYDNRAYSK GLTEVAMAGL ASTGVSVRNI GLATVPVAYW AQYFLKIKGV
CMGTASHNPN GWFGLKLGFD YTSTLVEEEI RELYSIIERE EFQVGQGAIE TVDGVIEAYQ
EDVVGRATLH RPLTVVVNCG NGTAGPINVP VLEKLGVKVI GQFIESDPTF PNHEPNPSLV
EFQRALSSKV LETKADLGIG FDADGDRLGL IDNLGQSFFS DKAFILLTRL ALEKEPGAKI
VFDVKSTQAL IDDIKAHGGV PVMWKTGHSF IKAKAKEVDA ALGGERSGHI FVRRGYYGYD
DALMAALKFL EYVSGQSKTV AELHDEVSTY AASPEIKAHC ADEIKEQVVA RIVQELKQEF
GPERVIDIDG ARVDFGDGWG LVRYSSNLPE LVLVFEAKTK ERMREIKELF RARLQKHPEV
GPFENE
//
