ID HEM1_HYPBU Reviewed; 411 AA. AC A2BJB7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 100. 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=Hbut_0206; OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae; OC Hyperthermus. OX NCBI_TaxID=415426; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5; RX PubMed=17350933; DOI=10.1155/2007/745987; RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., RA She Q., Garrett R.A., Klenk H.-P.; RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."; RL Archaea 2:127-135(2007). 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; CP000493; ABM80078.1; -; Genomic_DNA. DR RefSeq; WP_011821395.1; NC_008818.1. DR AlphaFoldDB; A2BJB7; -. DR SMR; A2BJB7; -. DR STRING; 415426.Hbut_0206; -. DR EnsemblBacteria; ABM80078; ABM80078; Hbut_0206. DR GeneID; 4782332; -. DR KEGG; hbu:Hbut_0206; -. DR eggNOG; arCOG01036; Archaea. DR HOGENOM; CLU_035113_0_0_2; -. DR OrthoDB; 4562at2157; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000002593; Chromosome. 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; 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; PTHR43013; GLUTAMYL-TRNA REDUCTASE; 1. DR PANTHER; PTHR43013:SF1; GLUTAMYL-TRNA REDUCTASE; 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. PE 3: Inferred from homology; KW NADP; Oxidoreductase; Porphyrin biosynthesis; Reference proteome. FT CHAIN 1..411 FT /note="Glutamyl-tRNA reductase" FT /id="PRO_0000335089" 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 99 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 104..106 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 110 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 179..184 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT SITE 89 FT /note="Important for activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" SQ SEQUENCE 411 AA; 45007 MW; C744C393B3D4C4FE CRC64; MPRLLEELTA VILTHRDAPL DVVGSFESRV GEAYQILRGV VDEAVVLATC NRFEVYALPR RGFVETVIGF LGEASRYARI LHGMDVVRHL FRVAAGLESA IIGENEILGQ VARAYEEARR RGVAGKYLGL LFSQAVRTGK LVRSRTRISY GNVGAPGAAV KLAREAAGGF DGKHVVVVGA GEAGSIMASL VREEAPTARI SIVNRSVDRA RELAGKVRGE AYGLDMLPKL LAAADVVLVA VTVNEPVIKR SMLEDVGRHL VVVDISNPPA VEQPIPSNVY YAGLRDVEKV IKEVLAVRIR EVPKAEAIVE EQVALLRKLW LKRGADEAIA EIMRYANRVM EEEVEELVSR LRGLGVDGAA LLVARSFAYS LTKKLLRPLI LYAHEAALEG SLSKLEEIAQ KYRDELARRQ H //