ID A0A0M9ZR19_9ACTN Unreviewed; 546 AA.
AC A0A0M9ZR19;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KOV69502.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KOV69502.1};
GN ORFNames=ADL00_11035 {ECO:0000313|EMBL:KOV69502.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV69502.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV69502.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV69502.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOV69502.1}.
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DR EMBL; LGDU01000081; KOV69502.1; -; Genomic_DNA.
DR RefSeq; WP_053757907.1; NZ_LGDU01000081.1.
DR AlphaFoldDB; A0A0M9ZR19; -.
DR PATRIC; fig|1519489.3.peg.2556; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000037758; Unassembled WGS sequence.
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:KOV69502.1};
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:UP000037758}.
FT DOMAIN 39..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..315
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 485..537
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 546 AA; 57501 MW; 7ED6B724D53526C2 CRC64;
MQHERAGRPA EPEDLVDVAR LVTAYYALHP DPADPGQRVA FGTSGHRGSS LASAFNDDHI
AATSQAICEY RAGQGIDGPL FLGADTHALS EPARVTALEV FAANDVSVLI DSADGYTPTP
AVSHAILSHN RGRTTGLADG VVVTPSHNPP ADGGFKYNPP SGGPAASAAT SWIQDRANEI
ITGGLKDVRR ITLTRALAAP GTGRHDFLGA YVADLSSVLD LDAIRAAGVH IGADPLGGAS
VAYWGRIAEE HRLDLTVVNP HTDPTWRFMT LDWDGKIRMD CSSPYAMASL IDRRDRFTIA
TGNDADADRH GIVTPDAGLM NPNHYLAAAI AYLYSHRDRW PADAGIGKTL VSSAMIDRVA
ADLGRRLVEV PVGFKWFVDG LVDGSLGFGG EESAGASFLR RDGSVWTTDK DGIILALLAS
EITAVTDRTP SQHYADMTAR FGEPAYARID APASREEKAL LGKLSPAQVT ADTLAGEAVT
AVLTEAPGNG APIGGIKVTT ANAWFAARPS GTEDVYKIYA ESFLGPDHLG QVQEEAKTVV
LAALGG
//
