ID A0A0G0RYG4_9BACT Unreviewed; 464 AA.
AC A0A0G0RYG4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KKR27495.1};
GN ORFNames=UT57_C0003G0009 {ECO:0000313|EMBL:KKR27495.1};
OS Microgenomates group bacterium GW2011_GWC1_39_7.
OC Bacteria.
OX NCBI_TaxID=1618515 {ECO:0000313|EMBL:KKR27495.1, ECO:0000313|Proteomes:UP000034535};
RN [1] {ECO:0000313|EMBL:KKR27495.1, ECO:0000313|Proteomes:UP000034535}
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:KKR27495.1}.
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DR EMBL; LBXH01000003; KKR27495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0RYG4; -.
DR Proteomes; UP000034535; 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 7..140
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 155..252
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 257..363
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 373..448
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 464 AA; 52124 MW; AD2354FD91546C0D CRC64;
MPLLKKTMFR EYDLRGRESE DELNDTSVYY LGRGFGAFLT KRNLKETVVG HDARATSESF
HANMIKGLTE SGIYVIDIGT VTTPMSYWSQ YFLKVKGLVM ITASHNPAGW NGVKFGTDFS
YTLLTDEMQE LYDIIAKDKF VDGKGSVTKK DIRDDYIRDL LSRASITKKF KILLNTGNGT
AGLFAPELLR QAGCEVVEHF TNVDPSYPNY TPNPDGTAMM EDTGKQTVAN KCDLGFAFDG
DGDRLGLVDE KGNIIWPDRY IILLSRLVLS KHPGAKIVFD VKVSEALPED IKAHGGVPIM
WKTGHSYIKA KLAEENAAMA GEMSGHIFFV DDFYGFDDAF FAGLKMLEYL STEDKPLSEI
IADTPYYVST PTIQVKTTDE DKYKVVDELV EEFKTEGYKV NDINGARVYI KDGWGLVRAS
SNTPTLVLRF ESKTQEGLDK IKDIFKQKLD RFDVVNKEWD TTGH
//
