ID A0A101NLZ6_9ACTN Unreviewed; 546 AA.
AC A0A101NLZ6;
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:KUM95357.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KUM95357.1};
GN ORFNames=AQI88_17150 {ECO:0000313|EMBL:KUM95357.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM95357.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM95357.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM95357.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
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:KUM95357.1}.
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DR EMBL; LMWL01000030; KUM95357.1; -; Genomic_DNA.
DR RefSeq; WP_066999413.1; NZ_KQ948022.1.
DR AlphaFoldDB; A0A101NLZ6; -.
DR STRING; 67285.AQI88_17150; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000054241; 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:KUM95357.1};
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:UP000054241}.
FT DOMAIN 39..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..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 491..537
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 546 AA; 57651 MW; DDF174A50C0177F3 CRC64;
MPHERAGRPA GPEDLVDVAR LVTAYYALHP DPADPGQRVA FGTSGHRGSS LATAFNEDHI
AATSQAICEY RAAQGVDGPL FLGADTHALS EPAKVTALEV FAASGVTVLV DSADGYTPTP
AVSHAILTYN RGRTSGLADG VVVTPSHNPP ADGGFKYNPP SGGPAASEAT SWIQDRANQI
IAGGLKDVQR LPYTRALAAD TTRRYDFLGT YVGDLPSVLD LDAIRAAGVR IGADPLGGAS
VAYWGRIAEQ HRIDLTVVNP HTDPTWRFMT LDWDGQIRMD CSSPYAMASL IERRDRFRIA
TGNDADADRH GIVTPDAGLM NPNHYLAVAI SYLYRHREQW PADAGIGKTL VSSTMIDRVA
ADLGRQLVEV PVGFKWFVDG LAAGTLGFGG EESAGASFLR RDGSVWTTDK DGIILALLAS
EITAVTDKTP SQHYADLTAR FGEPAYARID APATREQKAL LAKLSPAQVT ADTLAGEPVT
GVLTEAPGNG AAIGGIKVTT ANAWFAARPS GTEDVYKVYA ESFLGPDHLA QVQEEAKGVV
LAALGG
//
