ID A0A0B0PFE1_GOSAR Unreviewed; 495 AA.
AC A0A0B0PFE1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000313|EMBL:KHG25158.1};
GN ORFNames=F383_01671 {ECO:0000313|EMBL:KHG25158.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG25158.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KN431488; KHG25158.1; -; Genomic_DNA.
DR RefSeq; XP_017642436.1; XM_017786947.1.
DR RefSeq; XP_017642437.1; XM_017786948.1.
DR AlphaFoldDB; A0A0B0PFE1; -.
DR SMR; A0A0B0PFE1; -.
DR GeneID; 108483503; -.
DR KEGG; gab:108483503; -.
DR OMA; WPWSGGK; -.
DR OrthoDB; 313745at2759; -.
DR Proteomes; UP000032142; Unassembled WGS sequence.
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:UP000032142}.
FT DOMAIN 10..286
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 325..405
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 495 AA; 53177 MW; D683D026ADAAC237 CRC64;
MGSPAEPKRR VAFVLIDGLG DVSIPRFGNK TPLQAADVPT LDAIASAGVN GLMDPVEVGL
GCGSDTAHLS LLGYDPRVYY RGRGAFESMG AGLAMSPGDI AFKSNFATLD EKTGIVTSRR
ADRHFEEEGP ILCVALDRVK LPSFPEYEVR VRYATEHRCG VVVKGPRLSG NISGTDPLKD
NRLLLEAKAL DDTDEARHTA AVVNELSREI SKILVSHPLN AKRLAEGKSV ANVVLLRGCG
IRIEVPQFEK KHGLWPCMVA PTKIIAGLGL SLDIDILEAP GATGDYRTLL TSKATAIAKA
LSTPLQTSPS VFVPGEDEHK PGRSDGYDFG FLHIKAIDDA GHDKASVFKV KGLEAVDRAI
AQLAKLLWQA ESTGNFQYFI CVTGDHSTPV EYGDHSYEPV PFTICRLKDF VGAVGGESSV
LETSLDPFPL PTVKAGEDLN EAIGLEKGRK CKQVQAFCGD SVFEFNEIAA ARGCLGRFPG
GEMMGIIRKF LKLNA
//
