ID D2NS30_ROTMD Unreviewed; 420 AA.
AC D2NS30;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=RMDY18_06240 {ECO:0000313|EMBL:BAI64456.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64456.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64456.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64456.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64456.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64456.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
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; AP011540; BAI64456.1; -; Genomic_DNA.
DR RefSeq; WP_012903167.1; NC_013715.1.
DR AlphaFoldDB; D2NS30; -.
DR STRING; 680646.RMDY18_06240; -.
DR KEGG; rmu:RMDY18_06240; -.
DR eggNOG; COG0373; Bacteria.
DR HOGENOM; CLU_035113_4_1_11; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000001883; 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; 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:UP000001883}.
FT DOMAIN 9..165
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 181..303
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 319..414
FT /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF00745"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-1"
FT BINDING 50..53
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 118..120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 199..204
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 103
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-4"
SQ SEQUENCE 420 AA; 44761 MW; F3385EE3BBB7AD99 CRC64;
MSTYAFVASH HTVDLTTVAA LSAGASGVPD VLAADIARQL GVKGAVVLAT CNRLEMYVQL
HVSAHVHMVR ELIADSIAQT SGLDKELVNT SFDVYADEEA ARHLLTVASG LESAVVGERE
ITGQVRRALA AAQAKAQEDG VPLPGELVQL FEHAAHTARQ VGQHTALGAQ GRSIVSVALD
LADEVAEKDW STRRALIFGT GAYAGATIAA LRERGCTDIW VNSRSGRAAE FAAKREVSAV
PVDGMEQGMA EADVIIGCSG GSDPLLPEQI PAGHHTILDL ALSRDFDPSV ADLPNVELIT
LESVRLAAPE ETEESVATAT RIVESELAAF VSRQRSRTID SAIVALRSHT LDVLDSELEK
VRNQFGCGAA TEQFELAMRR MVKSLLHTPT VRAKKLASEG RAEDYVQALE TLYGIQVEES
//
