ID A0A0G3GU87_9CORY Unreviewed; 442 AA. AC A0A0G3GU87; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 24-JAN-2024, entry version 35. DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087}; DE Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087}; DE EC=1.2.1.70 {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087}; GN Name=hemA {ECO:0000256|HAMAP-Rule:MF_00087, GN ECO:0000313|EMBL:AKK04684.1}; GN ORFNames=CMUST_01675 {ECO:0000313|EMBL:AKK04684.1}; OS Corynebacterium mustelae. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK04684.1, ECO:0000313|Proteomes:UP000035199}; RN [1] {ECO:0000313|EMBL:AKK04684.1, ECO:0000313|Proteomes:UP000035199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK04684.1, RC ECO:0000313|Proteomes:UP000035199}; RX PubMed=26358597; RA Ruckert C., Eimer J., Winkler A., Tauch A.; RT "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM RT 45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis."; RL Genome Announc. 3:e01012-15(2015). RN [2] {ECO:0000313|Proteomes:UP000035199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199}; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated RT from various tissues of a male ferret with lethal sepsis."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) CC to glutamate 1-semialdehyde (GSA). {ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00001415, ECO:0000256|HAMAP- CC Rule:MF_00087, ECO:0000256|RuleBase:RU000584}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. CC {ECO:0000256|ARBA:ARBA00005059, ECO:0000256|HAMAP-Rule:MF_00087, CC ECO:0000256|RuleBase:RU000584}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00087}. CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family. CC {ECO:0000256|ARBA:ARBA00005916, ECO:0000256|HAMAP-Rule:MF_00087, CC ECO:0000256|RuleBase:RU000584}. 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; CP011542; AKK04684.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G3GU87; -. DR STRING; 571915.CMUST_01675; -. DR KEGG; cmv:CMUST_01675; -. DR PATRIC; fig|571915.4.peg.355; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000035199; 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 {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00087}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00087}; KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP- KW Rule:MF_00087}; Reference proteome {ECO:0000313|Proteomes:UP000035199}. FT DOMAIN 8..134 FT /note="Glutamyl-tRNA reductase N-terminal" FT /evidence="ECO:0000259|Pfam:PF05201" FT DOMAIN 162..289 FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA FT reductase" FT /evidence="ECO:0000259|Pfam:PF01488" FT DOMAIN 300..398 FT /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase FT dimerisation" FT /evidence="ECO:0000259|Pfam:PF00745" FT ACT_SITE 28 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-1" FT BINDING 27..30 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-2" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-2" FT BINDING 92..94 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-2" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-2" FT BINDING 173..178 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-3" FT SITE 77 FT /note="Important for activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-4" SQ SEQUENCE 442 AA; 47189 MW; 3BFB87C9C8AD1B2A CRC64; MDGDAKTHTA AELIDRPSLS EAMIVSTCNR FEVYCTTSSF HTGVSDVVDV LHRKSGVSVE TLRGCLYVRY ADAAAEHLMV VSAGMDSMVV GEQQIIGQVR TAYQQATDAG TVGPKLHSLV QAALHTGKRV HTETDIDTAG ASMVSFAFEE AIAQLGPVDI HQPFAGRTAL VLGAGAMASL AATQLGRLGI DELVVANRTR ERAERLAAHA REAGVAARVV DFADRRLALA EVDIAVSATG AQNFTITRTD IPSGHPLMLI DLSMPRDIDD AVTEGTMATL VNIERLHAIQ REDQGGDGAA LRIVAEELAD YSSAQRVKDV APAVTALRRH AAELIDTELL RLQGRTPDMA DAEFAEVANT VRRVVDKLLH QPTVRVKKLA AESGVVSYES ALQELFGLTG ESQSVRVELS ELPDAATLTT ETATAANTSI ETLRPQHQTQ GV //