ID M0ZVA1_SOLTU Unreviewed; 494 AA.
AC M0ZVA1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EnsemblPlants:PGSC0003DMT400008916};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400008916, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400008916}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400008916};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
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; Evidence={ECO:0000256|ARBA:ARBA00000370};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
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DR AlphaFoldDB; M0ZVA1; -.
DR STRING; 4113.M0ZVA1; -.
DR PaxDb; 4113-PGSC0003DMT400008916; -.
DR EnsemblPlants; PGSC0003DMT400008916; PGSC0003DMT400008916; PGSC0003DMG400003469.
DR Gramene; PGSC0003DMT400008916; PGSC0003DMT400008916; PGSC0003DMG400003469.
DR eggNOG; ENOG502QR26; Eukaryota.
DR InParanoid; M0ZVA1; -.
DR OMA; IAFRCNF; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M0ZVA1; baseline.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01676; Metalloenzyme; 2.
DR Pfam; PF10143; PhosphMutase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT DOMAIN 10..236
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 327..406
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 494 AA; 53042 MW; 38C090884A2732EF CRC64;
MVNLEQPKRR VAFVLIDGVG DVSLPRFGYR TPLQLAKIPN LDAIASAGVN GLMDPVEVGL
GCGSDTAHLS LLGYDPRVYY RGRGAFESMG AGLAMSPGDI AFKSNFATLD EETGIVVSRR
ADRHFEEEGP ILCAALDGMK LPSFPEYKIR VRYATEHRCG VVVKGPKLSG NISGTDPLKD
NRLLLQANPL DDTDEAKHTA AVVNELSKEI SRILLAHPLN AKRAAEGKNV ANLVLLRGCG
IRIEVAPFEK IHGLWPCMVA PTKIIAGLGL SLGIDILEAP GATGDYRTLL TSKATAIARA
LSAPLQSCPN VFVPGEDEHK PGRFDGYDFG FLHIKAIDDA GHDKASVFKV KGLEAVDCAI
GQLARLLWEA ESTGKFSYYL CITGDHSTPV EYGDHSFEPV PFALCSLKDF VSALGGESVL
SGISLDPFPL PSVQAGEDVD TGTRIEEDKN SKLQFFAGDL VDKFNEIAAA RGCLGRFPGS
EMMGIIKAYL KLEA
//
