ID A0A2M9JXE8_9ACTN Unreviewed; 542 AA.
AC A0A2M9JXE8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:PJN11559.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:PJN11559.1};
GN ORFNames=CG723_11720 {ECO:0000313|EMBL:PJN11559.1};
OS Streptomyces sp. CB01635.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN11559.1, ECO:0000313|Proteomes:UP000232157};
RN [1] {ECO:0000313|Proteomes:UP000232157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN11559.1}.
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DR EMBL; NNBL01000003; PJN11559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9JXE8; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000232157; 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:PJN11559.1};
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:UP000232157}.
FT DOMAIN 38..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 204..310
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 316..433
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 486..530
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 542 AA; 58002 MW; 5F1BABC9B34BF2DD CRC64;
MTERAGTQAR PEDLVDVDEL VDAYFTKVPD MDRPEQRVVF GTSGHRGSSL DGAFNERHIA
AITQAIVEYR TAEGITGPLF IGPDTHALSR PALDTALSVL AANGVRVFAD IHDSYVPTPA
LSHAILRWNS TAPDELGQAD GIVITPSHNP PRDGGFKYNP PHGGPADSTA TSWIARRANE
LLADGNRDVR TTKDVAPESY DFRERYVEEL SSVIDTDAIR ASGLRIGADP LGGASVHYWA
RIAKMYGLDL TVVNPQVDPT WRFMTLDWDG KIRMDPSSAP AMASVLAKRH DYDLLTGNDA
DADRHGIVTP DAGLMNPNHY LAVAIHYLAT HRTGWRSDAA IGKTLVSSAV IDRIVASLGR
ELLEVPVGFK WFVPGLVDGS VAFGGEESAG ASFVRKDGGV WTTDKDGILL ALLAAEITAV
TGKTPSQYYA ELAAEHGSSS YARVDAKATK RQKARLAELS GDAITADTLA GEPITGRLSH
APGNGAAIGG VKVTTENAWF AARPSGTEDV YKIYAESFRG PDHLAQVQTE AQSIVDAALA
ED
//
