GPMA1_ARATH
ID GPMA1_ARATH Reviewed; 334 AA.
AC Q9LM13; Q8L832; Q8LBD7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=BPG-dependent PGAM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=PGAM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=dPGM 1 {ECO:0000255|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Flags: Precursor;
GN Name=gpmA1 {ECO:0000255|HAMAP-Rule:MF_01039};
GN OrderedLocusNames=At1g22170 {ECO:0000312|Araport:AT1G22170};
GN ORFNames=F16L1.10 {ECO:0000312|EMBL:AAF87856.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP REVIEW.
RX PubMed=15333754; DOI=10.1104/pp.104.044610;
RA Wang R., Tischner R., Gutierrez R.A., Hoffman M., Xing X., Chen M.,
RA Coruzzi G., Crawford N.M.;
RT "Genomic analysis of the nitrate response using a nitrate reductase-null
RT mutant of Arabidopsis.";
RL Plant Physiol. 136:2512-2522(2004).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01039};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01039}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR EMBL; AC073942; AAF87856.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30205.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58755.1; -; Genomic_DNA.
DR EMBL; AY120773; AAM53331.1; -; mRNA.
DR EMBL; BT020337; AAV85692.1; -; mRNA.
DR EMBL; AY087272; AAM67325.1; -; mRNA.
DR PIR; C86354; C86354.
DR RefSeq; NP_001321168.1; NM_001332541.1.
DR RefSeq; NP_564161.1; NM_102067.3.
DR AlphaFoldDB; Q9LM13; -.
DR SMR; Q9LM13; -.
DR STRING; 3702.AT1G22170.1; -.
DR PaxDb; Q9LM13; -.
DR PRIDE; Q9LM13; -.
DR ProteomicsDB; 181750; -.
DR EnsemblPlants; AT1G22170.1; AT1G22170.1; AT1G22170.
DR EnsemblPlants; AT1G22170.2; AT1G22170.2; AT1G22170.
DR GeneID; 838822; -.
DR Gramene; AT1G22170.1; AT1G22170.1; AT1G22170.
DR Gramene; AT1G22170.2; AT1G22170.2; AT1G22170.
DR KEGG; ath:AT1G22170; -.
DR Araport; AT1G22170; -.
DR TAIR; locus:2015021; AT1G22170.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_1_2_1; -.
DR InParanoid; Q9LM13; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 804949at2759; -.
DR PhylomeDB; Q9LM13; -.
DR BioCyc; ARA:AT1G22170-MON; -.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:Q9LM13; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LM13; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Gluconeogenesis; Glycolysis; Isomerase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..334
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase 1"
FT /id="PRO_0000450719"
FT ACT_SITE 85
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 84..91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 188..191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 215..216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 259..260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 258
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT CONFLICT 56..57
FT /note="YD -> FN (in Ref. 5; AAM67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="H -> R (in Ref. 3; AAM53331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37295 MW; A3BDAEBC85A787EA CRC64;
MATATSHQSV VSFASLRSSP SSTISQCGFK IDSSLSFTSK KTNFCKIKAM ASSVSYDNTL
LSPSKTIPDN SQKKSNEAAL ILIRHGESLW NEKNLFTGCV DVPLTEKGVE EAIEAGKRIS
NIPVDVIFTS SLIRAQMTAM LAMIQHRRKK VPIILHDESE QAKTWSQVFS DETKNQSIPV
IPAWQLNERM YGELQGLNKQ ETAERYGKEQ VHEWRRSYDI PPPKGESLEM CAERAVAYFQ
DNIEPKLAAG KNVMIAAHGN SLRSIIMYLD KLTCQEVISL ELSTGIPLLY IFKEGKFMKR
GSPVGPTEAG VYAYTKRLAQ YRQKLEDDSE VLCA
