ID A0A179D3H2_9BACT Unreviewed; 452 AA.
AC A0A179D3H2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:OAQ20178.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:OAQ20178.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:OAQ20178.1};
GN ORFNames=TDIS_1680 {ECO:0000313|EMBL:OAQ20178.1};
OS Thermosulfurimonas dismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Thermosulfurimonas.
OX NCBI_TaxID=999894 {ECO:0000313|EMBL:OAQ20178.1, ECO:0000313|Proteomes:UP000078390};
RN [1] {ECO:0000313|EMBL:OAQ20178.1, ECO:0000313|Proteomes:UP000078390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S95 {ECO:0000313|EMBL:OAQ20178.1,
RC ECO:0000313|Proteomes:UP000078390};
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Slobodkin A.I., Ravin N.V.;
RT "Genome analysis of Thermosulfurimonas dismutans, the first thermophilic
RT sulfur-disproportionating bacterium of the phylum Thermodesulfobacteria.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU004326}.
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:OAQ20178.1}.
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DR EMBL; LWLG01000014; OAQ20178.1; -; Genomic_DNA.
DR RefSeq; WP_068671251.1; NZ_LWLG01000014.1.
DR AlphaFoldDB; A0A179D3H2; -.
DR STRING; 999894.TDIS_1680; -.
DR PATRIC; fig|999894.6.peg.1677; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000078390; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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; IPR016066; A-D-PHexomutase_CS.
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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OAQ20178.1};
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 7..138
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 254..366
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 370..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 452 AA; 50289 MW; 8EC053F34D84F7D1 CRC64;
MKVSPYIFRE YDIRGKVDED FTPEVVRVIG RAYGTVIRRR GGKQVLCGRD GRLSSPKLQQ
ALIEGITSAG ISVANIGMTP TPVMYFALHY FEGFDGGIQV TGSHNPPEFN GLKICVGRET
IYGAEIRALR DLIEKEDFES GQAEVTDLDA LGPYKEYLKK NIRLKRPLKV VLDPGNGVCA
LTAPEVFRAL GCEVECLFCE VDGTFPNHFP DPVVKENLET LRKKVLEIGA DFGVGYDGDG
DRLGVVNERG EILWGDQLMV LFARKLLAEH PGATVIGEVK CSQVMYDEIA RLGGRPLMWK
TGHSLIKNKM KETGALLAGE MSGHIFFAER WFGFDDGVYA SLRLAEIVSE SEKPLSELLA
DLPKTYNTPE IRTECPDEIK FKVVERLTKK LKEEGYEVVD VDGARVIFPD GWGLVRASNT
QPVLVLRFEA QSPERLEEIK ALIEGKLQEV MA
//
