ID HEM1_LIMRJ Reviewed; 421 AA. AC B2G9H5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087}; DE Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087}; DE EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087}; GN Name=hemA {ECO:0000255|HAMAP-Rule:MF_00087}; GN OrderedLocusNames=LAR_1591; OS Limosilactobacillus reuteri subsp. reuteri (strain JCM 1112) (Lactobacillus OS reuteri). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Limosilactobacillus. OX NCBI_TaxID=557433; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 1112; RX PubMed=18487258; DOI=10.1093/dnares/dsn009; RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., RA Hattori M.; RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus RT fermentum reveal a genomic island for reuterin and cobalamin production."; RL DNA Res. 15:151-161(2008). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) CC to glutamate 1-semialdehyde (GSA). {ECO:0000255|HAMAP-Rule:MF_00087}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00087}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure with CC each monomer consisting of three distinct domains arranged along a CC curved 'spinal' alpha-helix. The N-terminal catalytic domain CC specifically recognizes the glutamate moiety of the substrate. The CC second domain is the NADPH-binding domain, and the third C-terminal CC domain is responsible for dimerization. {ECO:0000255|HAMAP- CC Rule:MF_00087}. 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. {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family. CC {ECO:0000255|HAMAP-Rule:MF_00087}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP007281; BAG26107.1; -; Genomic_DNA. DR RefSeq; WP_011953572.1; NC_010609.1. DR AlphaFoldDB; B2G9H5; -. DR SMR; B2G9H5; -. DR KEGG; lrf:LAR_1591; -. DR HOGENOM; CLU_035113_2_2_9; -. DR UniPathway; UPA00251; UER00316. DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. 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:SF1; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1. DR Pfam; PF00745; GlutR_dimer; 1. DR Pfam; PF05201; GlutR_N; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 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. PE 3: Inferred from homology; KW NADP; Oxidoreductase; Porphyrin biosynthesis. FT CHAIN 1..421 FT /note="Glutamyl-tRNA reductase" FT /id="PRO_1000093148" FT ACT_SITE 50 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 49..52 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 109 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 114..116 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 189..194 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT SITE 99 FT /note="Important for activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" SQ SEQUENCE 421 AA; 47865 MW; 8967FAB42B1FAD0D CRC64; MYLMCVSLNY HQLPLDLREK FSFTKEEVPK ADKLLNDEKS ILENLLISTC NRTEVYAVVD QIHTGRYYIR RFLAEWFHYT IDDFTKFVTV TTKDAVAEHL FKVITGLDSL IKGEPQILGQ MKDAFQIATK EGTTGAILNH LFRQAITFSK RMHTKYRVSE LAQSSGQAGL HQIKMQFGSL EGKTLAVVGL GQIGKHTAYN ASNMGFSKVL LLNRTDSKAE QIATELQGVV EARPFNQLAT VVHNVDAAIF AATVKQPLFK ADEQISTMIV DLGVPRNVAV NSTKLKYYDV DHVHMILNSN DEKRRLMIQK IANEIPQEVN DFYIWEKQLH IVPVIRGLRE HSLRIEGEAY DSLLRKLPEL DSHERKVISK HMKSIVNQMI KGPIKEIKEL SVTPGATADI DFFCKIFGMD NLKVENQNND K //