ID A0A0Q7T8L2_9MICO Unreviewed; 547 AA.
AC A0A0Q7T8L2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KQY96805.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KQY96805.1};
GN ORFNames=ASD19_09645 {ECO:0000313|EMBL:KQY96805.1};
OS Microbacterium sp. Root53.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQY96805.1, ECO:0000313|Proteomes:UP000051407};
RN [1] {ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|Proteomes:UP000051407};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY96805.1, ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|EMBL:KQY96805.1,
RC ECO:0000313|Proteomes:UP000051407};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQY96805.1}.
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DR EMBL; LMFR01000025; KQY96805.1; -; Genomic_DNA.
DR RefSeq; WP_055993532.1; NZ_LMFR01000025.1.
DR AlphaFoldDB; A0A0Q7T8L2; -.
DR STRING; 1736553.ASD19_09645; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000051407; 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:KQY96805.1};
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:UP000051407}.
FT DOMAIN 38..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 322..439
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 485..541
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 58013 MW; B82073C731CF9799 CRC64;
MTSRAGLPAE ASDLIDVDEL INAYYDRVPD PSQPSQRVAF GTSGHRGSSL STSFNEQHIL
ATTQAIVDYR AEQGIQGPLF LGRDTHALSL PAERSAIEVL VANAVDVRID SRDSWVPTPA
LSLAILTFNR DLADADPGRA DGIVVTPSHN PPADGGFKYN PPHGGPADTD ATSWIAARAN
QLIEAGLEGV KRVRFADIDA GALGTYDFRD AYVRDLASII DIDAIREAGV RIGADPLGGA
SVEYWALIAE HYGLDLTVVN PDVDPTWRFM TLDWDEKIRM DPSSPSAMAS LVAKRSEYDI
LTGNDADADR HGIVTPDAGL MNPNHYLAVA IDYLFSHRPG WSSDAAVGKT LVSSMMIDKV
AASLGRTLLE VPVGFKWFVP GLIDGSVAFG GEESAGASFL RKDGTVWTTD KDGILLCLLA
AEILAVTGKT PSQRYAELEA EFGASAYQRV DAAATPEQKA ALGKLGPEAV TATTLAGEEI
VAKLTEAPGN GAAIGGLKVQ TASAWFAARP SGTEDVYKLY AESLRGEEHL RAVQDEARAV
VTAALGG
//
