HEM13_ARATH
ID HEM13_ARATH Reviewed; 524 AA.
AC Q9SJX1;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable glutamyl-tRNA reductase 3, chloroplastic;
DE EC=1.2.1.70;
DE Flags: Precursor;
GN Name=HEMA3; OrderedLocusNames=At2g31250; ORFNames=F16D14.9;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 IDENTIFICATION.
RX PubMed=15326282; DOI=10.1104/pp.104.042408;
RA Matsumoto F., Obayashi T., Sasaki-Sekimoto Y., Ohta H., Takamiya K.,
RA Masuda T.;
RT "Gene expression profiling of the tetrapyrrole metabolic pathway in
RT Arabidopsis with a mini-array system.";
RL Plant Physiol. 135:2379-2391(2004).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78520; EC=1.2.1.70;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC with the formation of a thioester intermediate between enzyme and
CC glutamate, and the concomitant release of tRNA(Glu). The thioester
CC intermediate is finally reduced by direct hydride transfer from NADPH,
CC to form the product GSA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000305}.
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DR EMBL; AC006593; AAD20670.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08514.1; -; Genomic_DNA.
DR PIR; D84718; D84718.
DR RefSeq; NP_180683.1; NM_128681.3.
DR AlphaFoldDB; Q9SJX1; -.
DR SMR; Q9SJX1; -.
DR STRING; 3702.AT2G31250.1; -.
DR iPTMnet; Q9SJX1; -.
DR PaxDb; Q9SJX1; -.
DR PRIDE; Q9SJX1; -.
DR ProteomicsDB; 230293; -.
DR EnsemblPlants; AT2G31250.1; AT2G31250.1; AT2G31250.
DR GeneID; 817682; -.
DR Gramene; AT2G31250.1; AT2G31250.1; AT2G31250.
DR KEGG; ath:AT2G31250; -.
DR Araport; AT2G31250; -.
DR TAIR; locus:2042516; AT2G31250.
DR eggNOG; ENOG502QQ1H; Eukaryota.
DR HOGENOM; CLU_035113_2_1_1; -.
DR InParanoid; Q9SJX1; -.
DR OMA; HTAPLEM; -.
DR OrthoDB; 571265at2759; -.
DR PhylomeDB; Q9SJX1; -.
DR BioCyc; ARA:AT2G31250-MON; -.
DR UniPathway; UPA00251; UER00316.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q9SJX1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJX1; baseline and differential.
DR Genevisible; Q9SJX1; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.460.30; -; 1.
DR HAMAP; MF_00087; Glu_tRNA_reductase; 1.
DR InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer.
DR InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR InterPro; IPR018214; GluRdtase_CS.
DR InterPro; IPR036453; GluRdtase_dimer_dom_sf.
DR InterPro; IPR036343; GluRdtase_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR Pfam; PF00745; GlutR_dimer; 1.
DR Pfam; PF05201; GlutR_N; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 1.
DR TIGRFAMs; TIGR01035; hemA; 1.
DR PROSITE; PS00747; GLUTR; 1.
PE 3: Inferred from homology;
KW Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase; Plastid;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..524
FT /note="Probable glutamyl-tRNA reductase 3, chloroplastic"
FT /id="PRO_0000422671"
FT ACT_SITE 130
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269..274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 524 AA; 58691 MW; E1DBE6D164EE1957 CRC64;
MAVSNASVVL SPNLETSSSW YHHNPSSSLD LIRIHTLPMN KMTRRGLIQR VRCETSPSSD
SSPLDKLKNS PAIDRYTRER SSIVVIGLSF HTSPLEMRER LAIPEAEWPL AITQLCALNH
IEEAAVLSTC NRIEIYVSAL SRYRGVKEVT EWMSKRSGIP VSDICQHRFL LYNKDATQHL
FQVSAGLESL VIGENQIQSQ VRKAEQVVKQ EGFGRIISTL FEKANKAGKR VRAQTNIASG
AVSVSSAAVE LALTKLPGSV SSAMMLVIGA GEMGKRIIEH LVAKGCTKMV VMNRSEDKVA
AIRKEMQSGV EIIYKPLDEI LACAAEANVI FTSTSSETPL FLKEHVEILP PCPADYARLF
VDISVPRNVG SCVAELDSAR VYNVDDLKEV VAANKEDRAR KSMEALPIIR EETIEFEGWR
DSLQTFPTIR KLRSKTERIR AECVEKLISK HGNGMDKKTR EAVEKQTRII VNNILDYPMK
HLRYDGTGSS KLRETLENMQ AVNRIYELDG ELLEEKIREK KDKK
