ID HEM1_PASMU Reviewed; 434 AA. AC P95525; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 27-MAR-2024, entry version 153. 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}; Synonyms=gltX1; GN OrderedLocusNames=PM0684; OS Pasteurella multocida (strain Pm70). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=2.5; RA Castrillon R.T.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). 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; Y10430; CAA71452.1; -; Genomic_DNA. DR EMBL; AE004439; AAK02768.1; -; Genomic_DNA. DR RefSeq; WP_010906790.1; NC_002663.1. DR AlphaFoldDB; P95525; -. DR SMR; P95525; -. DR STRING; 272843.PM0684; -. DR EnsemblBacteria; AAK02768; AAK02768; PM0684. DR KEGG; pmu:PM0684; -. DR PATRIC; fig|272843.6.peg.692; -. DR HOGENOM; CLU_035113_2_2_6; -. DR OrthoDB; 110209at2; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000000809; 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..434 FT /note="Glutamyl-tRNA reductase" FT /id="PRO_0000114052" 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 114 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 119..121 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 125 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT BINDING 199..204 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT SITE 104 FT /note="Important for activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087" FT CONFLICT 71..72 FT /note="TA -> AT (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="G -> D (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="M -> P (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" FT CONFLICT 171 FT /note="N -> S (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" FT CONFLICT 282 FT /note="A -> V (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="V -> A (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="A -> V (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" FT CONFLICT 379 FT /note="L -> F (in Ref. 1; CAA71452)" FT /evidence="ECO:0000305" SQ SEQUENCE 434 AA; 48408 MW; 648A624862C5E164 CRC64; MTILVIGINH KTASVAIREK VAFSAEKRVE ALAQIQQQAL AESAVILSTC NRTEVYFHHK AIPPQEAESW TARCMQWFAE IHQLSLDALA GCLYSQQNQQ AVLHLMRVAC GLDSLVLGEP QILGQVKDAY QLSKMYYQGQ NQPLSSEFSR LFQKTFSVAK RVRTETNIGG NAVSVAYGAC SLARQIFDSL KTLNVLLVGA GETIELTCRH LLRHGVQRIM IANRTFERAQ HLVTKLDGAE NVQVLALTQL QEGLNQADIV ISSTGSPTIL ITQDMVKIAQ KARCDLPMLL VDIAVPRDIE ESVGELDSIY HYTVDDLQTI IQRNLVEREK ASAQAWVIIQ QECADFFEWL KVHQFSNLIR SYRENAEDIR QILLEKALLA LRQGEDSEAV LQALSYKLTN KLLHSPTQVM NAMVKTGNST GLALFSSTLK SDVE //