ID A0A239GEK9_9MICO Unreviewed; 558 AA.
AC A0A239GEK9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SNS67569.1};
GN ORFNames=SAMN06309944_1278 {ECO:0000313|EMBL:SNS67569.1};
OS Micrococcales bacterium KH10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales.
OX NCBI_TaxID=1945885 {ECO:0000313|EMBL:SNS67569.1, ECO:0000313|Proteomes:UP000198369};
RN [1] {ECO:0000313|EMBL:SNS67569.1, ECO:0000313|Proteomes:UP000198369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH10 {ECO:0000313|EMBL:SNS67569.1,
RC ECO:0000313|Proteomes:UP000198369};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZPE01000001; SNS67569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239GEK9; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000198369; Unassembled WGS sequence.
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; IPR045244; PGM.
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
DR PANTHER; PTHR22573:SF57; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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:UP000198369}.
FT DOMAIN 38..186
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 217..326
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 332..453
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 497..552
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 558 AA; 58978 MW; ECB699D5403AD625 CRC64;
MDPRAGKVAE PSDLIDVDAL LGAYYDRRPD VEDPTQKVVF GTSGHRGSSL DAAFNEAHIV
AITAAIVEYR AMQGTNGPLF IGRDTHALSE PATNTALEVL AAAGVEVRID SRNSWTPTPA
VSHAILRANG VGSATGLRTS GTGLADGIVV TPSHNPPRDG GFKYNPPHGG PADSDATGWI
ANRANQWLRD GIGDIPRVSL RDALAADTTQ TYDFMGNYVD DLPSVINFDL IRTAGVRIGA
DPLGGAAVEY WAAIAERHNI DLTVVNPNVD PQWSFMTLDW DGKIRMDCSS PYSMASLVGR
MSGSGTNFDI ATGNDADSDR HGIVTPDAGL MNPNHYLATA ISYLYSGARP GWRPDAAIGK
TLVSSSLIDR LAAGIDRRLI EVPVGFKWFV PGLLDGSVGF GGEESAGASF LRFNGDVWTT
DKDGLILALL GSEIIATTGK SPSQLHRELV EKYGESWYAR VDAPASLEEK AKLSALTPAQ
VTSTTLAGEA ITAALTEAPG NGAKIGGLKV TTDNAWFAAR PSGTENVYKI YAESFVSADH
LAQVQSEARE VVAAALNS
//