ID A0A221RA43_9MICC Unreviewed; 551 AA.
AC A0A221RA43;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:ASN53774.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ASN53774.1};
GN ORFNames=CGQ25_00035 {ECO:0000313|EMBL:ASN53774.1};
OS Sinomonas sp. R1AF57.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=2020377 {ECO:0000313|EMBL:ASN53774.1, ECO:0000313|Proteomes:UP000199767};
RN [1] {ECO:0000313|EMBL:ASN53774.1, ECO:0000313|Proteomes:UP000199767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1AF57 {ECO:0000313|EMBL:ASN53774.1,
RC ECO:0000313|Proteomes:UP000199767};
RA Sastre D.E., Santos L., Kagohara E., Andrade L.H.;
RT "Draft Genome Sequence of Sinomonas sp., Isolated from Brazilian Amazon
RT Soils with Potential for Applications in Biocatalysis.";
RL Submitted (JUL-2017) 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; CP022463; ASN53774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221RA43; -.
DR Proteomes; UP000199767; 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:ASN53774.1};
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:UP000199767}.
FT DOMAIN 38..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..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 551 AA; 57984 MW; 0A6D232DDE96BBB5 CRC64;
MANRAGTVAL PSDLVDITAL LDAYYDVSPD LSDPGQRVAF GTSGHRGSSL KASFNEKHIA
AITQAIVEYR AGQGIQGPLF LAKDTHALSE PATNTALEVL AANNVQVLVD ARHGYTPTPS
ASHAILKYNA GRAENDPGRA DGIVVTPSHN PPADGGFKYN PPHGGPADTD ATGWIANRAN
ELLGANLSGV KRVPLADALS ADSTGQFDFL SSYVDDLPQV LNIAAIRDAG VRIGADPMGG
ASVDYWGEIG ERHHLDLTVV NPTVDPQWAF MTLDWDEKIR MDCSSPSAMA SLIQKVASGD
ARYDIATGND ADADRHGIVT PDAGLMNPNH YLSVAIDYLY RNRTGWRPDT VVGKTLVSSS
MIDRVAEGLG KPLVEVPVGF KWFVPGLLSG QGAFGGEESA GASFVKLDGG VWTTDKDGIL
LCLLASEIKA VTGKSPSELY GELTAKYGSP SYARIDAAAT REQKAKLGKL SASDVTATEL
AGEPITAKLT EAPGNGAKIG GLKVTTENAW FAARPSGTED VYKIYAESFK GDEHLAQVQA
EAKALVDSVI A
//
