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Database: UniProt
Entry: V7CKE1_PHAVU
LinkDB: V7CKE1_PHAVU
Original site: V7CKE1_PHAVU 
ID   V7CKE1_PHAVU            Unreviewed;       619 AA.
AC   V7CKE1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=PHAVU_002G096000g {ECO:0000313|EMBL:ESW29750.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW29750.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
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}.
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DR   EMBL; CM002289; ESW29750.1; -; Genomic_DNA.
DR   RefSeq; XP_007157756.1; XM_007157694.1.
DR   AlphaFoldDB; V7CKE1; -.
DR   STRING; 3885.V7CKE1; -.
DR   EnsemblPlants; ESW29750; ESW29750; PHAVU_002G096000g.
DR   GeneID; 18637461; -.
DR   Gramene; ESW29750; ESW29750; PHAVU_002G096000g.
DR   KEGG; pvu:PHAVU_002G096000g; -.
DR   eggNOG; KOG1220; Eukaryota.
DR   OMA; GQHGWVH; -.
DR   OrthoDB; 1775085at2759; -.
DR   Proteomes; UP000000226; Chromosome 2.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd03089; PMM_PGM; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR42946:SF2; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT   DOMAIN          72..216
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          266..351
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          355..455
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  67792 MW;  807211F9AB474D09 CRC64;
     MAASTSPNFS TSLDKNTHKT KFPSSAGKKI LHNKVGFSFS VPFNKSVGVK SFGTAKYDEV
     VVDDELEKIR RLQNGSDVRG VALEGEKGRK VDLTPPAVEA ISESFGEWVI NGLEAERGYP
     LENVRVSLGR DPRITGSKLS VAVFAGLSRA GCMVFDMGLA TTPACFMSTI LSPFAYDASI
     MMTASHLPYT RNGLKFFTKR GGLTSTEVEE ICDKAARKYA NRMTKVSTLL SVLPTKVDFM
     STYAMHLREI ITERINHPLY YDTPLQGFQI IVNAGNGSGG FFTWDVLDKL GADTFGSLHL
     TPDGMFPNHI PNPEDKTAMA LTRAAVLENS ADLGVVFDTD VDRSGVVDNK GNPINGDKLI
     ALMSAIVLRE HPGSTIVTDA RTSMALTRFI TDRGGNHCLY RVGYRNVIDK GVQLDSGGVE
     THLMMETSGH GALKENHFLD DGAYMVVKII IEMVRMKLAG SNEGIGSLIK DLEEPYESVE
     LRINIVSEPR HAKAKGSEAI QTFRNYIEEG RLRGWELDSC GDCWVSEGCL VDTNDDPAPI
     DAQMYRAKVS NDRHGQHGWV HMRQSIHNPN IAVNLQSSVP GGCLSMARAF RDEFLKASGV
     HTFLDITQVD KFAEKGSMA
//
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