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Database: UniProt
Entry: A0A120FIP0_9BRAD
LinkDB: A0A120FIP0_9BRAD
Original site: A0A120FIP0_9BRAD 
ID   A0A120FIP0_9BRAD        Unreviewed;       499 AA.
AC   A0A120FIP0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KWV47827.1};
GN   ORFNames=AS156_19565 {ECO:0000313|EMBL:KWV47827.1};
OS   Bradyrhizobium macuxiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV47827.1, ECO:0000313|Proteomes:UP000057737};
RN   [1] {ECO:0000313|EMBL:KWV47827.1, ECO:0000313|Proteomes:UP000057737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10303 {ECO:0000313|EMBL:KWV47827.1,
RC   ECO:0000313|Proteomes:UP000057737};
RA   Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT   "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
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}.
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:KWV47827.1}.
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DR   EMBL; LNCU01000112; KWV47827.1; -; Genomic_DNA.
DR   RefSeq; WP_066513687.1; NZ_LNCU01000112.1.
DR   AlphaFoldDB; A0A120FIP0; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000057737; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          26..158
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          175..272
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          278..390
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          411..486
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   499 AA;  54473 MW;  CE6CBB763C7C0303 CRC64;
     MFPKPKSVLV PNTYAFESEP MVKPTGFREY DARWLFNKEI NLMGVQALGM GLGALITELG
     VRQEIVTGHD FRGYSASIKY ALISGLVAAG CKVHDIGLAV TPMSYFAQFD LDVPCVAMVT
     ASHNDNGWTG VKMGANRPLT FGPDEMTRLK EIVLNAEFKN KAGGSYQFHE DYPARYIADL
     TNRPKLKRKL KVVAACGNGT AGAFAPQVLE AIGCEVIPLD TELDHTFPKY NPNPEDMEML
     HAIRDAVLAH KADVGLGFDG DGDRCGVVDN TGEEIFADKV GVMLARDMSA IHKNAQFVVD
     VKSTGLFVTD PVLSSQGATT VYWKTGHSYM KRRTNELGAL AGFEKSGHFF FNKPFGRGYD
     DGLVSAIAIC EMLDRAPGKS MADLKNALPK TWSSPTMSPH CADEAKYGVV DAVVKHFEAL
     QQKGGKVAGQ PIRDLVTVNG VRVTVEDGSW GLVRASSNKP ELVVVVESPA SERRMHDMFE
     AMDSVLRTHP EVGEYNQKI
//
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