ID HEM1_DESVH Reviewed; 440 AA. AC Q72C23; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 120. 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=DVU_1461; OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM OS B-1760 / Hildenborough). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Nitratidesulfovibrio. OX NCBI_TaxID=882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough; RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., RA Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). 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; AE017285; AAS95939.1; -; Genomic_DNA. DR RefSeq; WP_010938754.1; NZ_CABHLV010000001.1. DR RefSeq; YP_010680.1; NC_002937.3. DR AlphaFoldDB; Q72C23; -. DR SMR; Q72C23; -. DR IntAct; Q72C23; 1. DR STRING; 882.DVU_1461; -. DR PaxDb; 882-DVU_1461; -. DR EnsemblBacteria; AAS95939; AAS95939; DVU_1461. DR KEGG; dvu:DVU_1461; -. DR PATRIC; fig|882.5.peg.1360; -. DR eggNOG; COG0373; Bacteria. DR HOGENOM; CLU_035113_2_2_7; -. DR OrthoDB; 110209at2; -. DR PhylomeDB; Q72C23; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000002194; 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 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; 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. DR PROSITE; PS00747; GLUTR; 1. PE 3: Inferred from homology; KW NADP; Oxidoreductase; Porphyrin biosynthesis; Reference proteome. FT CHAIN 1..440 FT /note="Glutamyl-tRNA reductase" FT /id="PRO_0000114021" FT ACT_SITE 51 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 50..53 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 440 AA; 50045 MW; D166E5291B50E3BF CRC64; MERDIYLIGL NHRTAGVEVR ERFALTDCNV LEQGVVPIDD VVSEVLILST CNRVEILAVG RGPEVVSRVL RGWSAARGQC EHDLAPYVYT HKGPEAIRHL FRVASSLDSM VVGEPQILGQ LKDAYRKAIE RNCTRVILNR LLHKAFSVAK RVRTETGVAS SAVSISYAAV ELAKRIFGEM NQYKAMLIGA GEMAELAATH LLHAGISKIY VANRTFERGR ELARQFNGEA IHFEDLFERL ADADIIISST GAHEAIIRAR DIKDVLRRRK HRPMFFIDIA VPRDIDPDVN NLDNVYLYDI DDLKEVVEEN LAQRREEASK ALTIVEEETG KFGQWLRSLE LQPTIVDLIR RSERIAQDEL ARTLKRLGPV DDETRDALEA MLSSMVRKLN HEPITFLKRR HSEEDAGPRY IDIARRMFNL DDDNVPPDAH CDRRRHDEDN //