ID D7CY08_TRURR Unreviewed; 403 AA.
AC D7CY08;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|HAMAP-Rule:MF_00087};
DE Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087};
DE EC=1.2.1.70 {ECO:0000256|HAMAP-Rule:MF_00087};
GN Name=hemA {ECO:0000256|HAMAP-Rule:MF_00087};
GN OrderedLocusNames=Trad_0228 {ECO:0000313|EMBL:ADI13368.1};
OS Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / RQ-24).
OC Bacteria; Deinococcota; Deinococci; Trueperales; Trueperaceae; Truepera.
OX NCBI_TaxID=649638 {ECO:0000313|EMBL:ADI13368.1, ECO:0000313|Proteomes:UP000000379};
RN [1] {ECO:0000313|Proteomes:UP000000379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC {ECO:0000313|Proteomes:UP000000379};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Truepera radiovictris DSM 17093.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI13368.1, ECO:0000313|Proteomes:UP000000379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24
RC {ECO:0000313|Proteomes:UP000000379};
RX PubMed=21475591; DOI=10.4056/sigs.1563919;
RA Ivanova N., Rohde C., Munk C., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Rohde M.,
RA Goker M., Tindall B.J., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Truepera radiovictrix type strain (RQ-24).";
RL Stand. Genomic Sci. 4:91-99(2011).
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; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00087}.
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|HAMAP-Rule:MF_00087}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|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; CP002049; ADI13368.1; -; Genomic_DNA.
DR RefSeq; WP_013176748.1; NC_014221.1.
DR AlphaFoldDB; D7CY08; -.
DR STRING; 649638.Trad_0228; -.
DR KEGG; tra:Trad_0228; -.
DR eggNOG; COG0373; Bacteria.
DR HOGENOM; CLU_035113_1_0_0; -.
DR OrthoDB; 110209at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000000379; 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; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR InterPro; IPR036343; GluRdtase_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR43013; GLUTAMYL-TRNA REDUCTASE; 1.
DR PANTHER; PTHR43013:SF1; GLUTAMYL-TRNA REDUCTASE; 1.
DR Pfam; PF05201; GlutR_N; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR SUPFAM; SSF69742; Glutamyl tRNA-reductase catalytic, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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:UP000000379}.
FT DOMAIN 7..145
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 172..287
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT ACT_SITE 47
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 46..49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 104..106
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 177..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
SQ SEQUENCE 403 AA; 42904 MW; 04FC8C224DB68180 CRC64;
MERLALIGVS HRRGGAAALE AWQAAFKPPY SELAGLGFAE WVPIVTCNRW DVVVALPKTM
DVAQARALLT PTGQLCRPYA YTGDGALEQL TRIAASLDSL NPGEDQIMAQ VRSAFAAAQA
AGSTGPLTSF AFHTALRIAK KVRREVALAP LKTSLFSLAR PDLLRALPQG GSVAVLGAGE
MGSLAAKTLA SEPGFDLLIV NRSAPRARQL ARHLGARSSS LEAFLAAPPP VDALVCATPV
RALIDPLLVQ RLPELKLIID LGVPRNVHPE VIEASRVRVL DVDTLQAAGR TRREALQEKL
AAAEVILQEA LEGALEAWTE RQLGPSIQRL RQLYLATTLD ALGDGVGSEE AARLAHRFAH
VPVKGLRAVA RTYGLEAAQM FLAEAGLGEL RLGEAYAADA SRE
//
