ID   HEM12_ARATH             Reviewed;         530 AA.
AC   P49294; O04950; Q0WQP1; Q4V3B7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Glutamyl-tRNA reductase 2, chloroplastic;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Precursor;
GN   Name=HEMA2; OrderedLocusNames=At1g09940; ORFNames=F21M12.33;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=8605295; DOI=10.1007/bf00049321;
RA   Kumar A.M., Csankovszki G., Soell D.;
RT   "A second and differentially expressed glutamyl-tRNA reductase gene from
RT   Arabidopsis thaliana.";
RL   Plant Mol. Biol. 30:419-426(1996).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX   PubMed=12139011; DOI=10.1023/a:1016081114758;
RA   Ujwal M.L., McCormac A.C., Goulding A., Kumar A.M., Soell D., Terry M.J.;
RT   "Divergent regulation of the HEMA gene family encoding glutamyl-tRNA
RT   reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by
RT   sugars, but is independent of light and plastid signalling.";
RL   Plant Mol. Biol. 50:83-91(2002).
RN   [7]
RP   INDUCTION BY LIGHT, AND TISSUE SPECIFICITY.
RX   PubMed=11309145; DOI=10.1046/j.1365-313x.2001.00986.x;
RA   McCormac A.C., Fischer A., Kumar A.M., Soll D., Terry M.J.;
RT   "Regulation of HEMA1 expression by phytochrome and a plastid signal during
RT   de-etiolation in Arabidopsis thaliana.";
RL   Plant J. 25:549-561(2001).
RN   [8]
RP   FUNCTION, INDUCTION BY WOUNDING AND REACTIVE OXYGEN SPECIES, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17416636; DOI=10.1104/pp.107.100065;
RA   Nagai S., Koide M., Takahashi S., Kikuta A., Aono M., Sasaki-Sekimoto Y.,
RA   Ohta H., Takamiya K., Masuda T.;
RT   "Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and
RT   AtFC1, under stress conditions and their physiological functions in
RT   Arabidopsis.";
RL   Plant Physiol. 144:1039-1051(2007).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). Probably involved in wound-induced
CC       supply of heme to defensive hemoproteins outside plastids.
CC       {ECO:0000269|PubMed:12139011, ECO:0000269|PubMed:17416636,
CC       ECO:0000269|PubMed:8605295}.
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:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and flowers. Detected in leaves,
CC       hypocotyls and cotyledons. {ECO:0000269|PubMed:11309145,
CC       ECO:0000269|PubMed:12139011, ECO:0000269|PubMed:17416636,
CC       ECO:0000269|PubMed:8605295}.
CC   -!- INDUCTION: Not regulated by light. Up-regulated locally by wounding and
CC       reactive oxygen species. Not regulated by methyl jasmonate.
CC       {ECO:0000269|PubMed:11309145, ECO:0000269|PubMed:12139011,
CC       ECO:0000269|PubMed:17416636}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, but decreased heme content
CC       in roots. {ECO:0000269|PubMed:17416636}.
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; U27118; AAB01674.1; -; Genomic_DNA.
DR   EMBL; AC000132; AAB60749.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28519.1; -; Genomic_DNA.
DR   EMBL; BT023439; AAY56430.1; -; mRNA.
DR   EMBL; AK228651; BAF00558.1; -; mRNA.
DR   PIR; G86233; G86233.
DR   PIR; S65773; S65773.
DR   RefSeq; NP_172465.1; NM_100868.3.
DR   AlphaFoldDB; P49294; -.
DR   SMR; P49294; -.
DR   STRING; 3702.P49294; -.
DR   PaxDb; 3702-AT1G09940-1; -.
DR   ProteomicsDB; 230304; -.
DR   EnsemblPlants; AT1G09940.1; AT1G09940.1; AT1G09940.
DR   GeneID; 837528; -.
DR   Gramene; AT1G09940.1; AT1G09940.1; AT1G09940.
DR   KEGG; ath:AT1G09940; -.
DR   Araport; AT1G09940; -.
DR   TAIR; AT1G09940; HEMA2.
DR   eggNOG; ENOG502QQ1H; Eukaryota.
DR   HOGENOM; CLU_035113_2_1_1; -.
DR   InParanoid; P49294; -.
DR   OMA; YTERIIA; -.
DR   OrthoDB; 463at2759; -.
DR   PhylomeDB; P49294; -.
DR   BioCyc; ARA:AT1G09940-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G09940-MONOMER; -.
DR   UniPathway; UPA00251; UER00316.
DR   UniPathway; UPA00668; -.
DR   PRO; PR:P49294; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P49294; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
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:0006783; P:heme biosynthetic process; IMP:TAIR.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   GO; GO:0033014; P:tetrapyrrole biosynthetic process; IMP:TAIR.
DR   CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
DR   Gene3D; 3.30.460.30; Glutamyl-tRNA reductase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01035; hemA; 1.
DR   PANTHER; PTHR43120; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43120:SF14; GLUTAMYL-TRNA REDUCTASE 2, CHLOROPLASTIC; 1.
DR   Pfam; PF00745; GlutR_dimer; 1.
DR   Pfam; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   SUPFAM; SSF69742; Glutamyl tRNA-reductase catalytic, N-terminal domain; 1.
DR   SUPFAM; SSF69075; Glutamyl tRNA-reductase dimerization domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00747; GLUTR; 1.
DR   Genevisible; P49294; AT.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase; Plastid;
KW   Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..530
FT                   /note="Glutamyl-tRNA reductase 2, chloroplastic"
FT                   /id="PRO_0000013308"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         277..282
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            184
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        245
FT                   /note="A -> G (in Ref. 5; BAF00558)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        410
FT                   /note="D -> E (in Ref. 1; AAB01674)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   530 AA;  58292 MW;  0C0224296BA3D0A8 CRC64;
     MAVSSAFVVT PKLEKLLANH HNPTYSSSPA PLDVIGIRAL PMNNRNKRGL IQRARCEISP
     SNKAASISAL EQLKTSAIDR YTKERSSIVV IGLSIHTAPV EMREKLAIPE AEWPRAIAEL
     CGLNHIEEAA VLSTCNRMEI YVLALSQHRG VKEVTEWMSK TSGIPVSEIC QHRFLLYNKD
     VTQHIFEVSA GLDSLVLGEG QILAQVKQVV KVGQGVNGFG RNISGLFKHA ITVGKRVRTE
     TNIAAGAVSV SSAAVELALM KLPESSHASS ARMLVVGAGK MGKLVIKHLV AKGCTKMVVV
     NRSEEKVAAV RNEMPPGVEI IYKPLDEMLS CAAEADVVFT STASETPLFL KEQVETLPPV
     RDARLFVDIS VPRNVGSCVA EIDGTRVFNV DDLKEVVAAN KEDRVRKAMD AQAIITDESK
     HFEAWRDSLE TVPTIKKLRG YTERIIAAEI EKSLPKMGID MNKKMRKTVD DLIRGIVNKL
     LHGPMQHLRC DGNDSRTLSE TLDNMQALNR MYGLDAEILE EKIRAKVEKK
//