ID A0A109IN85_9ACTN Unreviewed; 545 AA.
AC A0A109IN85;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SCG50062.1};
GN ORFNames=GA0070623_1773 {ECO:0000313|EMBL:SCG50062.1};
OS Micromonospora rifamycinica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG50062.1, ECO:0000313|Proteomes:UP000198226};
RN [1] {ECO:0000313|EMBL:SCG50062.1, ECO:0000313|Proteomes:UP000198226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG50062.1,
RC ECO:0000313|Proteomes:UP000198226};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; LT607752; SCG50062.1; -; Genomic_DNA.
DR RefSeq; WP_067303476.1; NZ_LT607752.1.
DR AlphaFoldDB; A0A109IN85; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000198226; Chromosome i.
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}.
FT DOMAIN 40..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 321..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 489..537
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 545 AA; 57709 MW; 61A386857450C464 CRC64;
MAHPRAGQPA EPADLVDVPR LVTAYYAEHP DPDDPAQQVS FGTSGHRGSS LRNAFNSDHI
LAVTQALCDY RREQGLTGPL FLARDTHALS APAEADALEV LAGNGVTVLR DSRDGYTPTP
ALSHAVLTHN RGRTDGLADG IVITPSHNPP DDGGFKYNPT NGGPADTDVT KWIQDRANAI
LAAGLKEVRR IPYARARAAD TTGTYDFLAG YVDDLPSVLD IDAIRDAGVR IGADPLGGAS
VGYWGEIAER HRLDLTVINP LVDPTWRFMT LDGDGKIRMD CSSPNAMASL IAARDRFQVS
TGNDADADRH GIVTPDGGLM NPNHYLAVAI GHLFRTRSQW GPAAAVGKTL VSSSMIDRIA
ADLGRPLLEV PVGFKWFVPG LLDGSVGFGG EESAGASFLR RDGSTWTTDK DGILLCLLAA
EIIATTGRTP SEHYAALTDR FGAPAYARID APADREQKAV LGRLSPEQVT ATELAGEPIT
ATLTSAPGNG APIGGLKVTT GSGWFAARPS GTEDVYKIYA ESFQGPEHLA RIQEEAKSLV
DGVLG
//