ID E8V4S1_TERSS Unreviewed; 547 AA.
AC E8V4S1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:ADV81475.1};
GN OrderedLocusNames=AciPR4_0641 {ECO:0000313|EMBL:ADV81475.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV81475.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV81475.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002467; ADV81475.1; -; Genomic_DNA.
DR RefSeq; WP_013567208.1; NC_014963.1.
DR AlphaFoldDB; E8V4S1; -.
DR STRING; 401053.AciPR4_0641; -.
DR KEGG; tsa:AciPR4_0641; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_0; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000006844; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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; 3.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006844}.
FT DOMAIN 40..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 322..442
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 470..540
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 547 AA; 58782 MW; A47C1440E11320A4 CRC64;
MSLNPNAGKL PSPASLANLP RLTSEYFAIL PDVEQPAQRV AFGTSGHRGS ALLGSFNEQH
ILAITQAICE HRAGEKIDGP LFLAMDTHAL SEPAFISALE VLAANGVTTL IDSERRYTPT
PALSHAILTY NHGRATGLSD GIVITPSHNP PVDGGFKYNP PNGGPADTNV TKWVENRAND
LLRAHLEGVK RITFQKAINA STTQKHDFLS EYVGHLEDVL DLDIIRSSGL SFAVDPLGGA
GVDYWPRIAE QYKLPLTVLS TEVDQTFRFM TLDWDGKIRM DCSSPYAMAS MIAKKDKFDV
AFACDTDHDR HGIVARSVGL LNPNHYLAVA IQYLFTNRSG WGKDAAIGKT LVSSSMIDRV
AAGIGRKLLE VPVGFKWFVD GLMDGSLGFG GEESAGASFL RKDGGPWSTD KDGPIMGLLS
AEMTARTGKD PGQLYADLTA KYGEPVYQRI DAAATREEKA KLSKLSPEQV KVKDLAGEPI
TQVLTNAPGN GAAIGGLKVA TESGWFAARP SGTEDVYKIY AESFKGEDHL KQIQTEAKAL
VDAALAG
//
