HEM11_CUCSA
ID HEM11_CUCSA Reviewed; 552 AA.
AC P93111;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glutamyl-tRNA reductase 1, chloroplastic;
DE Short=GluTR;
DE EC=1.2.1.70;
DE Flags: Precursor;
GN Name=HEMA1;
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Aonagajibai; TISSUE=Cotyledon;
RX PubMed=8934625; DOI=10.1104/pp.110.4.1223;
RA Tanaka R., Yoshida K., Nakayashiki T., Masuda T., Tsuji H., Inokuchi H.,
RA Tanaka A.;
RT "Differential expression of two hemA mRNAs encoding glutamyl-tRNA reductase
RT proteins in greening cucumber seedlings.";
RL Plant Physiol. 110:1223-1230(1996).
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Primarily in cotyledons and hypocotyls of greening
CC cucumber seedlings.
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; D50407; BAA08910.1; -; mRNA.
DR PIR; T10186; T10186.
DR RefSeq; NP_001267503.1; NM_001280574.1.
DR AlphaFoldDB; P93111; -.
DR SMR; P93111; -.
DR STRING; 3659.XP_004148403.1; -.
DR EnsemblPlants; KGN62779; KGN62779; Csa_2G372750.
DR GeneID; 101220615; -.
DR Gramene; KGN62779; KGN62779; Csa_2G372750.
DR KEGG; csv:101220615; -.
DR eggNOG; ENOG502QQ1H; Eukaryota.
DR OMA; QMKVFPR; -.
DR UniPathway; UPA00251; UER00316.
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-KW.
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 2: Evidence at transcript level;
KW Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase; Plastid;
KW Porphyrin biosynthesis; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..552
FT /note="Glutamyl-tRNA reductase 1, chloroplastic"
FT /id="PRO_0000013309"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 150..153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215..217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292..297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 200
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 60895 MW; 9C7A72AF24FF00F5 CRC64;
MAVSTSFSGA KLEALLFKSA SNSSSTRNLS SSHLPGFCKS IRTRRILFQR TGVSSFTPFK
CELASSDVLV QNDEIDPPKS SNLSALEQLK TSAVDRYTKE RSSIVVIGLS IHTTPVEMRE
KLAIPEAEWP RAIGELCGLN HIEEAAVLST CNRMEIYVVA LSQHRGVKEV TEWMSKTSGI
PVSEICQHRF LLYNNDATQH IFEVSAGLDS LVLGEGQILA QVKQVVKVGQ GVAGFGRNIS
GLFKHAITVG KRVRTETNIA AGAVSVSSAA VELALMKLPE PSHATARMLV IGAGKMGKLV
IKHLVAKGCT KMVVVNRSEE RVTAIREEMK DVEIIYKPLT EMLSCTAEAD VIFTSTASES
LLFTKEQVKD LPPVGHDVGG LRLFIDISVP RNVGACINNL EDVRVYNVDD LKEVVAANKE
DRLRKAMEAQ SIITEESKQF EAWRDSLETV PTIKKLRAYA ERIRTAELEK CLSKMGDDIP
KKTRRAVDDL SRGIVNKLLH GPMQHLRCDG SDSRTLSETL ENMHALNRMF SLETEIAVLE
QKIRAKVEQN QK
