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Database: UniProt
Entry: A0A2G8T8T3_9BURK
LinkDB: A0A2G8T8T3_9BURK
Original site: A0A2G8T8T3_9BURK 
ID   A0A2G8T8T3_9BURK        Unreviewed;       543 AA.
AC   A0A2G8T8T3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=CR105_24300 {ECO:0000313|EMBL:PIL42414.1};
OS   Massilia eurypsychrophila.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1485217 {ECO:0000313|EMBL:PIL42414.1, ECO:0000313|Proteomes:UP000230390};
RN   [1] {ECO:0000313|EMBL:PIL42414.1, ECO:0000313|Proteomes:UP000230390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 30074 {ECO:0000313|EMBL:PIL42414.1,
RC   ECO:0000313|Proteomes:UP000230390};
RA   Wang H.;
RT   "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT   isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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:PIL42414.1}.
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DR   EMBL; PDOC01000027; PIL42414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8T8T3; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000230390; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR045244; PGM.
DR   PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 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   Magnesium {ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230390}.
FT   DOMAIN          14..151
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          184..286
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          295..407
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   543 AA;  57328 MW;  F067F2E61D2137CE CRC64;
     MTIHSVASTP YAGQRPGTSG LRKKVSEFLQ PGYLENFVEA IFQTIGDCRG QTLVLGGDGR
     YFNRTAVGVI LQMAAAHGVG RVLVGQGGIL STPAVSCVIR KHAAFGGIVL SASHNPGGPE
     GDFGIKYNIG NGGPAPEKIT EALYLYTQTN ALYRISDAAV PDLDTVGVSR IEQMDVEVID
     PVSDYAELMA SLFDFAAIKA LFAGGFTMRF DAMHAVCGPY AHAILEGMLG APAGTVINGT
     PLEDFGGHHP DPNPVNAAEL IAEMFGAAAP DFGAASDGDA DRNMIVARGL AVTPSDSLAI
     IAANAKLAPG YRAGLAGIAR SMPTSTAADR VAKSLGIPCY ETPTGWKYFG NLLDAGMVTL
     CGEESYGTGS SHIREKDGLW AVLFWLNLLA ASGKPAATLV REHWATFGRN YYSRHDYEAV
     DAQAAEAMMA HLRGQLGQLA GRQLDGFTVA LADDFVYTDP VDLSVTSKQG VRIVMTDGSR
     IVFRLSGTGT EGATIRLYLE KYEADQARHA IDPQQALAGL ATIAANLSQL KTRTGRDHPT
     IVT
//
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