ID H5SAM8_9CHLR Unreviewed; 474 AA.
AC H5SAM8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:BAL53214.1};
GN ORFNames=HGMM_F05B10C36 {ECO:0000313|EMBL:BAL53214.1}, HGMM_F19G07C23
GN {ECO:0000313|EMBL:BAL54772.1};
OS uncultured Chloroflexota bacterium.
OC Bacteria; Chloroflexota; environmental samples.
OX NCBI_TaxID=166587 {ECO:0000313|EMBL:BAL53214.1};
RN [1] {ECO:0000313|EMBL:BAL53214.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL53214.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
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}.
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DR EMBL; AP011651; BAL53214.1; -; Genomic_DNA.
DR EMBL; AP011699; BAL54772.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SAM8; -.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05800; PGM_like2; 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 PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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 SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
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 6..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 164..265
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 273..379
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 430..465
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 474 AA; 52722 MW; F91BF4CB2BCF41CB CRC64;
MSFHIRFGTD GWRGVIAEDY TFDNVRRAAQ GFASYLLKQG KRDEWVVIGY DKRFQSENFA
LAAAEVLTGN GLRVYLTQEA TPTPVIAYAV VHQRACGAIN ITASHNPPTD NGFKVRDEHG
GAIPPQGLKE IESLIPPEVQ AVKRLPANEA EAQGRLVRFD AAPAYIEHIQ TLIDLEPLRQ
AGLTLLVDPM WGNGAGWFPR LLGGGKTRII EIHNVRNPIF PEMKRPEPIP PNINIGLQAT
REHAADALLI TDGDADRFGL GDEHGQFVNQ LRVYALLAYY LLEVRGERGP IVKTLSTTTM
LNRLGEMYGV PVYETGVGFK YVAPKMLEVN ALIGGEESGG YAFRNHVPER DGILAGLYLL
DFMVRTGRRP SQLLELLFQK LGQEYFYDRV DSPFSGDRAA REQRILQANP QTIGGLRVTG
LSTLDGFQFH LEDGGWMLIR FSGTEPILRV YCETTHREKV QAILEDGLRI AGVK
//
