ID A0A0G3HES0_9CORY Unreviewed; 553 AA.
AC A0A0G3HES0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:AKK09617.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:AKK09617.1};
GN Name=celB {ECO:0000313|EMBL:AKK09617.1};
GN ORFNames=CTEST_11005 {ECO:0000313|EMBL:AKK09617.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK09617.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK09617.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK09617.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-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}.
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DR EMBL; CP011545; AKK09617.1; -; Genomic_DNA.
DR RefSeq; WP_047253748.1; NZ_JAASJB010000011.1.
DR AlphaFoldDB; A0A0G3HES0; -.
DR STRING; 136857.CTEST_11005; -.
DR KEGG; cted:CTEST_11005; -.
DR PATRIC; fig|136857.5.peg.2180; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000035540; Chromosome.
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:AKK09617.1};
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:UP000035540}.
FT DOMAIN 40..186
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 216..321
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..447
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 491..545
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 553 AA; 58815 MW; 8B984189AA071922 CRC64;
MAHERAGQLA RPEDLIDIAE VVTAYYTRIP DVENPDQQVA FGTSGHRGSS LDTAFNENHI
LATTQAIVDY RRANSIGGPV FIGRDPHALS EPAMISALEV LLGNNITVLV DDRGRYTPTP
AVSHAILAHN AGLAGGVTGT DPLRADGVVI TPSHNPPRDG GFKYNPPSGG PADTDATDWI
AARANDYLRA GLDGVSRVAV AGVLDPRAER YNYQDTYIAD LPNVVNIDAI RGSGLSIGAD
PMGGASVDYW GAIADAHGLN LTVVNPLVDA TWRFMTLDTD GKIRMDCSSP DSMASLVHNR
DKFDIATGND ADADRHGIVT PDAGLMNPNH YLAVAIEYLF GNRPGWSPDT AVGKTLVSSS
MIDRVVGNLG RRLVEVPVGF KWFVPGLIDG TIGFGGEESA GASFLRHNGT VWSTDKDGLI
MDLLAAEITA VTGKTPSQRY AELAAEYGAP FYARTDAEAN REQKAVLKNL SPEQVTADTL
AGEAITAKLT NAPGNGAPIG GLKVTTESAW FAARPSGTED KYKIYAESFR GEEHLREVQQ
EAEALVSDVL KNA
//
