GLUBP_ARATH
ID GLUBP_ARATH Reviewed; 317 AA.
AC Q9LU39; Q8LAE4;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Glutamyl-tRNA reductase-binding protein, chloroplastic {ECO:0000303|PubMed:22180625};
DE Short=AtGluTRBP {ECO:0000303|PubMed:22180625};
DE Short=GluTR-binding protein {ECO:0000303|PubMed:22180625};
DE AltName: Full=Protein PROTON GRADIENT REGULATION 7 {ECO:0000303|PubMed:20657737};
DE Flags: Precursor;
GN Name=GLUTRBP {ECO:0000303|PubMed:22180625};
GN Synonyms=PGR7 {ECO:0000303|PubMed:20657737};
GN OrderedLocusNames=At3g21200 {ECO:0000312|Araport:AT3G21200};
GN ORFNames=MXL8.5 {ECO:0000312|EMBL:AAL32732.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20657737; DOI=10.1371/journal.pone.0011688;
RA Jung H.S., Okegawa Y., Shih P.M., Kellogg E., Abdel-Ghany S.E., Pilon M.,
RA Sjolander K., Shikanai T., Niyogi K.K.;
RT "Arabidopsis thaliana PGR7 encodes a conserved chloroplast protein that is
RT necessary for efficient photosynthetic electron transport.";
RL PLoS ONE 5:E11688-E11688(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEMA1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22180625; DOI=10.1105/tpc.111.086421;
RA Czarnecki O., Hedtke B., Melzer M., Rothbart M., Richter A., Schroter Y.,
RA Pfannschmidt T., Grimm B.;
RT "An Arabidopsis GluTR binding protein mediates spatial separation of 5-
RT aminolevulinic acid synthesis in chloroplasts.";
RL Plant Cell 23:4476-4491(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 42-317, FUNCTION, AND SUBUNIT.
RX PubMed=24753615; DOI=10.1073/pnas.1400166111;
RA Zhao A., Fang Y., Chen X., Zhao S., Dong W., Lin Y., Gong W., Liu L.;
RT "Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with
RT its stimulator protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6630-6635(2014).
CC -!- FUNCTION: Involved in the regulation of glutamyl-tRNA reductase (GluTR)
CC which is important for the synthesis and distribution of 5-
CC aminolevulinate, a precursor in heme and chlorophyll biosynthesis
CC (PubMed:22180625). Stimulates GluTR activity and regulates glutamate-1-
CC semialdehyde release. May play a role in heme metabolism
CC (PubMed:24753615). Necessary for efficient photosynthetic electron
CC transport in chloroplasts (PubMed:20657737).
CC -!- SUBUNIT: Interacts with HEMA1 (PubMed:22180625, PubMed:24753615) and
CC forms a heterotetramer of two GLUTRBP and two HEMA1 subunits
CC (PubMed:24753615). {ECO:0000269|PubMed:22180625,
CC ECO:0000269|PubMed:24753615}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:20657737, ECO:0000269|PubMed:22180625}.
CC Note=Detected at low levels in thylakoids.
CC {ECO:0000269|PubMed:20657737, ECO:0000269|PubMed:22180625}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth, slightly pale green leaves,
CC reduced levels of chlorophyll and heme, and low non-photochemical
CC quenching (NPQ). {ECO:0000269|PubMed:20657737,
CC ECO:0000269|PubMed:22180625}.
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DR EMBL; AB023045; BAB01711.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76475.1; -; Genomic_DNA.
DR EMBL; AY062654; AAL32732.1; -; mRNA.
DR EMBL; BT002574; AAO00934.1; -; mRNA.
DR EMBL; AY087867; AAM65419.1; -; mRNA.
DR RefSeq; NP_566678.1; NM_113015.3.
DR PDB; 4N7R; X-ray; 2.80 A; C/D=42-317.
DR PDB; 5CHE; X-ray; 3.20 A; C/D=42-317.
DR PDB; 5YJL; X-ray; 2.70 A; C/D=42-317.
DR PDBsum; 4N7R; -.
DR PDBsum; 5CHE; -.
DR PDBsum; 5YJL; -.
DR AlphaFoldDB; Q9LU39; -.
DR SMR; Q9LU39; -.
DR BioGRID; 7005; 1.
DR IntAct; Q9LU39; 1.
DR STRING; 3702.AT3G21200.1; -.
DR PaxDb; Q9LU39; -.
DR PRIDE; Q9LU39; -.
DR ProteomicsDB; 247403; -.
DR EnsemblPlants; AT3G21200.1; AT3G21200.1; AT3G21200.
DR GeneID; 821673; -.
DR Gramene; AT3G21200.1; AT3G21200.1; AT3G21200.
DR KEGG; ath:AT3G21200; -.
DR Araport; AT3G21200; -.
DR TAIR; locus:2094741; AT3G21200.
DR eggNOG; ENOG502QT0S; Eukaryota.
DR HOGENOM; CLU_051089_0_0_1; -.
DR InParanoid; Q9LU39; -.
DR OMA; KSTFNCM; -.
DR OrthoDB; 1468491at2759; -.
DR PhylomeDB; Q9LU39; -.
DR PRO; PR:Q9LU39; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LU39; baseline and differential.
DR Genevisible; Q9LU39; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IPI:TAIR.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:TAIR.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:TAIR.
DR GO; GO:0070455; P:positive regulation of heme biosynthetic process; IMP:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0033014; P:tetrapyrrole biosynthetic process; IMP:TAIR.
DR Gene3D; 2.30.110.10; -; 1.
DR Gene3D; 3.20.180.10; -; 1.
DR InterPro; IPR019595; DUF2470.
DR InterPro; IPR037119; Haem_oxidase_HugZ-like_sf.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF10615; DUF2470; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll biosynthesis; Chloroplast; Heme biosynthesis;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 43..317
FT /note="Glutamyl-tRNA reductase-binding protein,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430936"
FT CONFLICT 27
FT /note="F -> L (in Ref. 4; AAM65419)"
FT CONFLICT 102
FT /note="V -> I (in Ref. 4; AAM65419)"
FT CONFLICT 154
FT /note="R -> K (in Ref. 4; AAM65419)"
FT CONFLICT 162
FT /note="K -> E (in Ref. 4; AAM65419)"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4N7R"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:5YJL"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4N7R"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 166..179
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:5YJL"
FT TURN 199..203
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:5YJL"
FT HELIX 270..288
FT /evidence="ECO:0007829|PDB:5YJL"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:5YJL"
SQ SEQUENCE 317 AA; 35463 MW; B38BDD80F2632F8A CRC64;
MQLQTQSFAL NLLPSPNFAK PIERREFISL KRDPSRPISL RCSVSTTLDT PATASTHKPF
PAEVSRSIME LSSVGTLSTL THDGWPLGVG VRFAVDKDGT PVLCLNRSVS PDKRSALHVQ
LEQCGLRTPQ CTIQGSIGRP GDDTVLKRLS ATWREKFGEE VKEDSLYVVA VDRVLQMEDF
MEDGIWVASS DYKNASPDPL RDIAEDIVNQ INANNMEDIF RFCNVYVDLD FVVSETKMIW
MDRLGFDLRV WSPRGVYDVR IPFPMEVTDE KGAKSSFNGM SQLAWEVEKS YCPADFNKVK
LLKQVVGSSH SHKGGGQ
