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PMGI_RICCO
ID   PMGI_RICCO              Reviewed;         556 AA.
AC   P35493;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
DE            Short=BPG-independent PGAM;
DE            Short=Phosphoglyceromutase;
DE            EC=5.4.2.12;
DE   AltName: Full=PGAM-I;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=cv. Baker 296; TISSUE=Endosperm;
RX   PubMed=8260624; DOI=10.1007/bf00021818;
RA   Huang Y., Blakeley S.D., McAleese S.M., Fothergill-Gilmore L.A.,
RA   Dennis D.T.;
RT   "Higher-plant cofactor-independent phosphoglyceromutase: purification,
RT   molecular characterization and expression.";
RL   Plant Mol. Biol. 23:1039-1053(1993).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.12;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Found ubiquitously in germinating seed.
CC   -!- DEVELOPMENTAL STAGE: Expression most important during germination, it
CC       decreases during development.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000305}.
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DR   EMBL; X70652; CAA49995.1; -; mRNA.
DR   PIR; S49647; S49647.
DR   AlphaFoldDB; P35493; -.
DR   SMR; P35493; -.
DR   STRING; 3988.XP_002519975.1; -.
DR   PRIDE; P35493; -.
DR   eggNOG; KOG4513; Eukaryota.
DR   UniPathway; UPA00109; UER00186.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16010; iPGM; 1.
DR   Gene3D; 3.40.1450.10; -; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR011258; BPG-indep_PGM_N.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR036646; PGAM_B_sf.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   PANTHER; PTHR31637; PTHR31637; 1.
DR   Pfam; PF06415; iPGM_N; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001492; IPGAM; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   SUPFAM; SSF64158; SSF64158; 1.
DR   TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; Isomerase; Manganese;
KW   Metal-binding.
FT   CHAIN           1..556
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000212113"
FT   ACT_SITE        78
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         25
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         167..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         283..286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         427
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         431
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         468
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         469
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         498
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
SQ   SEQUENCE   556 AA;  60818 MW;  F6456D7D8067862C CRC64;
     GEFTWKLADH PKLPKGKTIA MVVLDGWGEA KPDQYNCIHV AETPTMDSFK KTAPERWRLI
     KAHGTAVGLP TEDDMGNSEV GHNALGAGRI YAQGAKLVDL ALASGKIYEG EGFKYVKECF
     DKGTLHLIGL LSDGGVHSRL DQLQLLLKGA AEHGAKRIRV HVLTDGRDVI DGTSVGFAET
     LEKDLENLRE KGVDAQVASG GGRMYVTMDR YENDWNVVKR GWDAQVLGEA PYKFKSAVEA
     IKKLREEPKA NDQYLPPFVI VDENGKPVGP IVDGDAVVTI NFRADRMVML AKALEYENFD
     TFDRVRFPKI HYAGMLQYDG ELKLPSHYLV SPPEIERTSG EYLVHNGVHT FACSETVKFG
     HVTFFWNGNR SGYFNPEMEE YVEIPSDVGI TFNVQPKMKA IEIAEKARDA ILSGKFQQVR
     VNIPNGDMVG HTGDVEATVV GCKAADEAVK MIIDAIEQVG GIYVVTADHG NAEDMVKRDK
     SGKPMADKSG KIQILTSHTL QPVPIAIGGP GLTPGVRFRS DIPTGGLANV AATVMNLHGF
     EAPSDYEPTL IEAVDN
 
 
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