ID A0A0S8JHJ4_9BACE Unreviewed; 494 AA.
AC A0A0S8JHJ4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KPL09169.1};
DE Flags: Fragment;
GN ORFNames=AMS26_23200 {ECO:0000313|EMBL:KPL09169.1};
OS Bacteroides sp. SM23_62.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL09169.1, ECO:0000313|Proteomes:UP000050819};
RN [1] {ECO:0000313|EMBL:KPL09169.1, ECO:0000313|Proteomes:UP000050819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL09169.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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, 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:KPL09169.1}.
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DR EMBL; LJUP01000360; KPL09169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8JHJ4; -.
DR PATRIC; fig|1703352.3.peg.3676; -.
DR Proteomes; UP000050819; Unassembled WGS sequence.
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; cd05799; PGM2; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 5..98
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 124..232
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 238..359
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPL09169.1"
SQ SEQUENCE 494 AA; 54911 MW; F3DE9521BC1A0B92 CRC64;
LPRIKVAIAH DSRNNSRLFA ETTARIFAAN GIKAYLFDDL RPTPELSFAI RHFGCQSGVI
ITASHNPKEY NGYKVYWDDG GQIIAPHDEN IIGEVNRISG IDEVKFEGDP ALIETIGASI
DDLYTDKLAT LSLSPEAIRQ QHDLKIVYTP IHGTGVKLVP MALKKFGFTR IINVPEQDEV
NGDFPTVHSP NPEETAALAM GLQKAEEEGA ELVMATDPDA DRVGIAVRDD RGKLILLNGN
QTGSLLYYYL IRKWSENGKL TGIQYVAKTI VTTELLADIA RKFGVEIFNV LTGFKFIADI
IRREEGKKEF IIGSEESYGY LAGDFVRDKD AVMSCALIAE TAAWARIQGK TLYELLLDIY
LEFGLYLEQL SYIVKKGKSG AEIIAGMMQN YRETPPAGLA GSPVVLIHDY QSSKTLDTIT
GKSSPIELPR SNVLQFITED HTKVSIRPSG TEPKIKFYFS VKGSLENRQD YPAQKTRLEQ
KINTLRKELG ITEL
//
