ID A0A0G3GU87_9CORY Unreviewed; 442 AA. AC A0A0G3GU87; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 17-FEB-2016, entry version 5. DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|HAMAP-Rule:MF_00087, ECO:0000256|RuleBase:RU000584, ECO:0000256|SAAS:SAAS00318939}; DE Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087}; DE EC=1.2.1.70 {ECO:0000256|HAMAP-Rule:MF_00087, ECO:0000256|RuleBase:RU000584, ECO:0000256|SAAS:SAAS00318939}; 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; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK04684.1, ECO:0000313|Proteomes:UP000035199}; RN [1] {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, RT isolated 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- CC tRNA(Glu) to glutamate 1-semialdehyde (GSA). {ECO:0000256|HAMAP- CC Rule:MF_00087, ECO:0000256|SAAS:SAAS00317143}. CC -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) + CC tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. {ECO:0000256|HAMAP- CC Rule:MF_00087, ECO:0000256|RuleBase:RU000584, CC ECO:0000256|SAAS:SAAS00041126}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step CC 1/2. {ECO:0000256|HAMAP-Rule:MF_00087, CC ECO:0000256|RuleBase:RU000584, ECO:0000256|SAAS:SAAS00041161}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00087, CC ECO:0000256|SAAS:SAAS00317140}. CC -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure CC with each monomer consisting of three distinct domains arranged CC along a curved 'spinal' alpha-helix. The N-terminal catalytic CC domain specifically recognizes the glutamate moiety of the CC substrate. The second domain is the NADPH-binding domain, and the CC third C-terminal domain is responsible for dimerization. CC {ECO:0000256|HAMAP-Rule:MF_00087}. CC -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a CC nucleophile attacking the alpha-carbonyl group of tRNA-bound CC glutamate with the formation of a thioester intermediate between CC enzyme and glutamate, and the concomitant release of tRNA(Glu). CC The thioester intermediate is finally reduced by direct hydride CC transfer from NADPH, to form the product GSA. {ECO:0000256|HAMAP- CC Rule:MF_00087}. CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family. CC {ECO:0000256|HAMAP-Rule:MF_00087, 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 EnsemblBacteria; AKK04684; AKK04684; CMUST_01675. DR KEGG; cmv:CMUST_01675; -. DR KO; K02492; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000035199; Chromosome. DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. 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; SSF51735; SSF51735; 1. DR SUPFAM; SSF69075; SSF69075; 1. DR SUPFAM; SSF69742; SSF69742; 1. DR TIGRFAMs; TIGR01035; hemA; 1. DR PROSITE; PS00747; GLUTR; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035199}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00087, ECO:0000256|PIRSR:PIRSR000445- KW 3, ECO:0000256|RuleBase:RU000584, ECO:0000256|SAAS:SAAS00436218}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00087, KW ECO:0000256|RuleBase:RU000584, ECO:0000256|SAAS:SAAS00436233, KW ECO:0000313|EMBL:AKK04684.1}; KW Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00087, KW ECO:0000256|RuleBase:RU000584, ECO:0000256|SAAS:SAAS00436220}; KW Reference proteome {ECO:0000313|Proteomes:UP000035199}. FT DOMAIN 14 134 GlutR_N. {ECO:0000259|Pfam:PF05201}. FT DOMAIN 162 288 Shikimate_DH. {ECO:0000259|Pfam:PF01488}. FT DOMAIN 300 398 GlutR_dimer. {ECO:0000259|Pfam:PF00745}. FT NP_BIND 173 178 NADP. {ECO:0000256|HAMAP-Rule:MF_00087, FT ECO:0000256|PIRSR:PIRSR000445-3}. FT REGION 27 30 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00087, ECO:0000256|PIRSR: FT PIRSR000445-2}. FT REGION 92 94 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00087, ECO:0000256|PIRSR: FT PIRSR000445-2}. FT ACT_SITE 28 28 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_00087, ECO:0000256|PIRSR:PIRSR000445- FT 1}. FT BINDING 87 87 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00087, ECO:0000256|PIRSR:PIRSR000445- FT 2}. FT BINDING 98 98 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00087, ECO:0000256|PIRSR:PIRSR000445- FT 2}. FT SITE 77 77 Important for activity. FT {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 //