HEM12_ARATH
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 03-AUG-2022, entry version 162.
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 localy 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.AT1G09940.1; -.
DR PaxDb; P49294; -.
DR PRIDE; P49294; -.
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; locus:2024392; AT1G09940.
DR eggNOG; ENOG502QQ1H; Eukaryota.
DR HOGENOM; CLU_035113_2_1_1; -.
DR InParanoid; P49294; -.
DR OMA; YTERIIA; -.
DR OrthoDB; 571265at2759; -.
DR PhylomeDB; P49294; -.
DR BioCyc; ARA:AT1G09940-MON; -.
DR BioCyc; MetaCyc:AT1G09940-MON; -.
DR UniPathway; UPA00251; UER00316.
DR UniPathway; UPA00668; -.
DR PRO; PR:P49294; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P49294; baseline and differential.
DR Genevisible; P49294; AT.
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 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 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
