ID M0QNF3_9ACTN Unreviewed; 561 AA.
AC M0QNF3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Putative phosphoglucomutase {ECO:0000313|EMBL:GAC69811.1};
GN ORFNames=GS4_28_00590 {ECO:0000313|EMBL:GAC69811.1};
OS Gordonia soli NBRC 108243.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC69811.1, ECO:0000313|Proteomes:UP000011666};
RN [1] {ECO:0000313|EMBL:GAC69811.1, ECO:0000313|Proteomes:UP000011666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC69811.1,
RC ECO:0000313|Proteomes:UP000011666};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL Submitted (JAN-2013) 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:GAC69811.1}.
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DR EMBL; BANX01000028; GAC69811.1; -; Genomic_DNA.
DR RefSeq; WP_007623244.1; NZ_BANX01000028.1.
DR AlphaFoldDB; M0QNF3; -.
DR STRING; 1223545.GS4_28_00590; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000011666; 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; 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; 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 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};
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:UP000011666}.
FT DOMAIN 46..182
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..305
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 318..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 506..544
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 561 AA; 58216 MW; C9ED715335B921B5 CRC64;
MATPVPDDLA TRVAAWIDGD PDPTTRAELS ASSADDLAER FADTLRFGTA GLRGPVRAGP
GGMNVAVVIR TTAALAAWLH RSVDGTDGAR TVVVGHDART GSVEFATAAG EVLAGAGFDV
VALPGHSPTP LVAHACRALD AVAAVQITAS HNPPADNGYK VYLRGGAQLI PPADREIEEL
IADVGPANRV RRTQVASDDR GTAASAAYLR RLRERFGGPD GPDVRIALTA LHGVGGPLAL
AALVGAGITD VHVVPEQFDP DPAFPTVRFP NPEEPGAADR VLALAEDVGA DLAIALDPDA
DRCAIGVRRN GLWQMLTGDE TGALVGAHLL ADGFSGDAGA TARAGDERPV VASTIVSGSL
LAAVAAAADA RHVRTLTGFK WLVRAGEPLR YAYEEAIGHC VDPDAVRDKD GISAAVVAAR
IAQLHRRAGT TVDDGLDELF RRHGVHVTTQ QSIRVTDLSV IGRLMSTLRT DPPHSLAGIT
VVAEDLAVRT DALRTDAVEF TGRSDDGVAL RVIARPSGTE PKLKYYVEVI APPEVADIAT
TRAELTDLAA RVAADLPADA G
//