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Database: UniProt
Entry: A0A3G8JUN9_9ACTN
LinkDB: A0A3G8JUN9_9ACTN
Original site: A0A3G8JUN9_9ACTN 
ID   A0A3G8JUN9_9ACTN        Unreviewed;       560 AA.
AC   A0A3G8JUN9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AZG48633.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:AZG48633.1};
GN   Name=pgm {ECO:0000313|EMBL:AZG48633.1};
GN   ORFNames=D7316_05252 {ECO:0000313|EMBL:AZG48633.1};
OS   Gordonia insulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG48633.1, ECO:0000313|Proteomes:UP000271469};
RN   [1] {ECO:0000313|EMBL:AZG48633.1, ECO:0000313|Proteomes:UP000271469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG48633.1,
RC   ECO:0000313|Proteomes:UP000271469};
RA   Kim Y.S., Kim S.B.;
RT   "Gordonia insulae sp. nov., isolated from an island soil.";
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; CP033972; AZG48633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G8JUN9; -.
DR   KEGG; gom:D7316_05252; -.
DR   Proteomes; UP000271469; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:AZG48633.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271469}.
FT   DOMAIN          53..193
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          224..332
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          336..456
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          504..554
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   560 AA;  59675 MW;  6AFC96A9A981B6AA CRC64;
     MSPFGSVAQW QNCGMAHPRA GTPALPEDLI DVAAVERAYY EKVPDPEDPL QQVLFGTSGH
     RGSSLDSAFN EAHILATTQA IVEYRKSAGI TGPLFIGFDT HALSIPAWRS ALEVLTANEV
     DVYIAENEKF TPTPAVSFAI LRFNQANPGV LADGIVVTPS HNPPRDGGFK YNPPNGGPAD
     TSITSVVARR ANELLAGKLA GVKRIPFERA RSSEFIHDYP FTATYVDHLH EVVDMTAIRD
     AGVHIGADPL GGASVGYWAE IGFRYNLQNL TVVNPTVDPT FRFMTLDTDG KIRMDCSSPN
     AMASLISARD TYDIATGNDA DSDRHGIVTP DGGLMNPNHY LAVAIDYLFT HRPGWGGDAA
     VGKTLVSSSL IDRVVGGIGR PLVEVPVGFK WFVDGLLNGS IAFGGEESAG ASFLTFDGAP
     WSTDKDGIIM ALLASEILAK TGKTPSQRYR ELAERYGESA YARIDAPASR AQKALLAKLS
     ADQVTATELA GEPITAILTE APGNGAPIGG LKVTTENAWF AARPSGTEDV YKIYAESFNG
     ADHLATVQAQ AQELVDSVLV
//
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