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Database: UniProt
Entry: A0A0X3RPN5_9ACTN
LinkDB: A0A0X3RPN5_9ACTN
Original site: A0A0X3RPN5_9ACTN 
ID   A0A0X3RPN5_9ACTN        Unreviewed;       546 AA.
AC   A0A0X3RPN5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KUJ33554.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:KUJ33554.1};
GN   ORFNames=ADL25_44755 {ECO:0000313|EMBL:KUJ33554.1};
OS   Streptomyces sp. NRRL F-5122.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ33554.1, ECO:0000313|Proteomes:UP000054048};
RN   [1] {ECO:0000313|Proteomes:UP000054048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (OCT-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:KUJ33554.1}.
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DR   EMBL; LMWH01000305; KUJ33554.1; -; Genomic_DNA.
DR   RefSeq; WP_059133740.1; NZ_LMWH01000305.1.
DR   AlphaFoldDB; A0A0X3RPN5; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000054048; 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:KUJ33554.1};
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:UP000054048}.
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          489..535
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   546 AA;  57893 MW;  7435051D4D6847C4 CRC64;
     MQHERAGRPA GPEDLIDVPR LVTAYYALHP DPAEPGQRVA FGTSGHRGSS LATAFNEDHI
     AATSQAICEY RARQGTDGPL FLGADTHALS EPARITALEV FAANDVTVLL DTEDGYTPTP
     AVSHAILTHN RARTSGPADG VVVTPSHNPP GDGGFKYNPP SGGPAGSDAT SWIQDRANEI
     IAGGMKDVRR VTYSRALAAP GTGRYDFLGA YVSDLPSVLD LDAIRGAGVR IGADPLGGAS
     VDYWGRIAEQ HRLDLTVVNP LTDPTWRFMT LDWDGKIRMD CSSPYAMASL IEQRDRFRIA
     TGNDADADRH GIVTPDAGLM NPNHYLATAI SYLYSHRTQW PAEAGVGKTL VSSGMIDRVA
     ADLGRPLVEV PVGFKWFVDG LVDGSLGFGG EESAGASFLR RDGSVWTTDK DGIILALLAS
     EITAVTDRTP SEHYAALTAR FGEPAYARID APASREDKAR LAKLSPAQVS ADTLAGEPVT
     AVLTEAPGNG APIGGIKVAT ANAWFAARPS GTEDVYKIYA ESFLGSDHLR QVQDEAKVVV
     LRALGG
//
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