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Database: UniProt
Entry: A0A0Q6BLI1_9PROT
LinkDB: A0A0Q6BLI1_9PROT
Original site: A0A0Q6BLI1_9PROT 
ID   A0A0Q6BLI1_9PROT        Unreviewed;       469 AA.
AC   A0A0Q6BLI1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KQT41786.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:KQT41786.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:KQT41786.1};
GN   ORFNames=ASG34_09470 {ECO:0000313|EMBL:KQT41786.1};
OS   Methylophilus sp. Leaf416.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT41786.1, ECO:0000313|Proteomes:UP000050891};
RN   [1] {ECO:0000313|EMBL:KQT41786.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41786.1,
RC   ECO:0000313|Proteomes:UP000050891};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT41786.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41786.1,
RC   ECO:0000313|Proteomes:UP000050891};
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:KQT41786.1}.
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DR   EMBL; LMQS01000003; KQT41786.1; -; Genomic_DNA.
DR   RefSeq; WP_055829875.1; NZ_LMQS01000003.1.
DR   AlphaFoldDB; A0A0Q6BLI1; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000050891; 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:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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   PRINTS; PR00509; PGMPMM.
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:KQT41786.1};
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}.
FT   DOMAIN          10..142
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          159..255
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          260..372
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          398..458
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   469 AA;  50998 MW;  CACC9EC15218A438 CRC64;
     MTSTALPGSI FKAYDIRGIV DETLTAEIVR LIGLALGTQV QALGEQSICV GYDGRLSSPA
     LARALAEGIL QTGVDVISLG LVTTPMLYFA THYLPRSTSG VMITGSHNPP QYNGLKMVLA
     GETLSSEAIQ ALRQQIDQQQ FYLSSHPGKT STYDIYPAYQ QTIVEDIQLA RTMRVVVDCG
     NGVAGAYAQA LFEALGCMVD PLFCEVDGNF PNHHPDPVEA KNLQDVIARL QTGDAELGLA
     FDGDGDRLGV VTKSGQIIRS DRQLMLFIED VLAHQPGSSV VFDVKSTRYL SQWTRKHGGK
     PVIWKTGHSL MKAKIRETSA AIGGELSGHL FFNDQKQGKQ RWFGFDDGLY SAARLLEIVS
     RVSDASAVLE ALPDSVNTPE LQIVMAEGEP HALIAQLQET AAFPAAVEVI DIDGLRVEYA
     DGFGLIRASN TTPVLVLRFE ADNQKALARI KNIFRELLLN ARPDLKIPF
//
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