GPMA2_ARATH
ID GPMA2_ARATH Reviewed; 332 AA.
AC F4I8M8; Q8GX43; Q9SGZ6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=BPG-dependent PGAM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=PGAM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=dPGM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
DE Flags: Precursor;
GN Name=gpmA2 {ECO:0000255|HAMAP-Rule:MF_01039};
GN OrderedLocusNames=At1g78050 {ECO:0000312|Araport:AT1G78050};
GN ORFNames=F28K19.30 {ECO:0000312|EMBL:AAF17689.1};
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] OF 128-332.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-332.
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 [5]
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).
RN [6]
RP INDUCTION BY NITRITE AND NITRATE.
RC STRAIN=cv. Columbia;
RX PubMed=17951451; DOI=10.1104/pp.107.108944;
RA Wang R., Xing X., Crawford N.;
RT "Nitrite acts as a transcriptome signal at micromolar concentrations in
RT Arabidopsis roots.";
RL Plant Physiol. 145:1735-1745(2007).
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 -!- INDUCTION: Highly but transiently induced by nitrite and nitrate.
CC {ECO:0000269|PubMed:17951451}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17689.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC43054.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009243; AAF17689.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36062.1; -; Genomic_DNA.
DR EMBL; AK118445; BAC43054.1; ALT_INIT; mRNA.
DR EMBL; BT003728; AAO39956.1; -; mRNA.
DR PIR; F96809; F96809.
DR RefSeq; NP_177928.2; NM_106454.4.
DR AlphaFoldDB; F4I8M8; -.
DR SMR; F4I8M8; -.
DR STRING; 3702.AT1G78050.1; -.
DR PaxDb; F4I8M8; -.
DR PRIDE; F4I8M8; -.
DR ProteomicsDB; 212327; -.
DR EnsemblPlants; AT1G78050.1; AT1G78050.1; AT1G78050.
DR GeneID; 844140; -.
DR Gramene; AT1G78050.1; AT1G78050.1; AT1G78050.
DR KEGG; ath:AT1G78050; -.
DR Araport; AT1G78050; -.
DR TAIR; locus:2029371; AT1G78050.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_1_2_1; -.
DR InParanoid; F4I8M8; -.
DR OMA; MSHQAIG; -.
DR OrthoDB; 804949at2759; -.
DR UniPathway; UPA00109; UER00186.
DR PRO; PR:F4I8M8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I8M8; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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 GO; GO:0010167; P:response to nitrate; IEP:UniProtKB.
DR GO; GO:0080033; P:response to nitrite; IEP:UniProtKB.
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..332
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase 2"
FT /id="PRO_0000450720"
FT ACT_SITE 86
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 189
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 85..92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 98..99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 189..192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 216..217
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 260..261
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 259
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 332 AA; 37216 MW; 74B0A58D2C1377A5 CRC64;
MATSTTMSHQ AIGSVVSQRP FKASQFLKEP LNNVPMKFRQ KRFKIEATAS QISVVDNTFL
SPSPSKNKPH ESKKKSNEAA LILIRHGESL WNEKNLFTGC VDVPLTQKGV GEAIEAGKKI
SNIPVDLIFT SSLIRAQMTA MLAMTQHRRK KVPIILHNES VKAKTWSHVF SEETRKQSIP
VIAAWQLNER MYGELQGLNK KETAERYGTQ QVHEWRRSYE IPPPKGESLE MCAERAVAYF
EDNIKPELAS GNNVMIAAHG NSLRSIIMYL DDLTSQEVTT LDLSTGVPLL YIFKEGKFMK
RGSPVGSTEA GVYAYTKRLA QYREKLDAAA TI
