ID A0A3M8K905_9CORY Unreviewed; 552 AA.
AC A0A3M8K905;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:RNE49713.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:RNE49713.1};
GN ORFNames=C5L39_05130 {ECO:0000313|EMBL:RNE49713.1};
OS Corynebacterium alimapuense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1576874 {ECO:0000313|EMBL:RNE49713.1, ECO:0000313|Proteomes:UP000266975};
RN [1] {ECO:0000313|EMBL:RNE49713.1, ECO:0000313|Proteomes:UP000266975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 69366 {ECO:0000313|EMBL:RNE49713.1,
RC ECO:0000313|Proteomes:UP000266975};
RA Claverias F., Gonzales-Siles L., Salva-Serra F., Inganaes E., Molin K.,
RA Cumsille A., Undabarrena A., Couve E., Moore E.R.B., Gomila M., Camara B.;
RT "Corynebacterium alimpuense sp. nov., a marine obligate actinomycete
RT isolated from sediments of Valparaiso bay, Chile.";
RL Submitted (FEB-2018) 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:RNE49713.1}.
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DR EMBL; PTJO01000003; RNE49713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8K905; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000266975; 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:RNE49713.1};
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:UP000266975}.
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 489..545
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 552 AA; 58603 MW; 0954B066FBEEC34D CRC64;
MAHERAGQLA RPEDLIDIAE VVTAYYTRTP DVADPDQQVA FGTSGHRGSS LDTAFNENHI
LATTQAIVDY RRANSIGGPV FVGRDPHALS EPAMISALEV LLANDIAVLV DDRGRYTPTP
AVSHAILAHN SVLAGGVTGT DPKRADGIVI TPSHNPPRDG GFKYNPPSGG PADTDATDWI
AERANAYLRA GLDGVQRTSV SGVLDSRAQR YNYLDTYVAD LPNVVDMKAI RDSGLSIGAD
PMGGASVDYW GAIAQAHGLN LTVVNPEVDA TWRFMTLDTD GKIRMDCSSP NAMASLIGNR
DKYDISTGND ADADRHGIVT PDHGLMNPNH YLAVAIEYLF AHRPGWAADT AVGKTLVSSS
MIDRVVAELG RKLIEVPVGF KWFVPGLIDG SVGFGGEESA GASFLRHDGS VWSTDKDGLI
LDLLAAEITA VTGKTPSQRY AELAEQYGAP SYARADAEAS REQKAVLKNL SPEQVTADTL
AGEPITAKLT AAPGNGAAIG GLKVTTENAW FAARPSGTED KYKIYAESFR GDEHLRQVQA
EAQALVSEVL GG
//
