ID G4RKU1_THETK Unreviewed; 405 AA.
AC G4RKU1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 ECO:0000313|EMBL:CCC82186.1};
GN OrderedLocusNames=TTX_1559 {ECO:0000313|EMBL:CCC82186.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC82186.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC82186.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(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}.
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DR EMBL; FN869859; CCC82186.1; -; Genomic_DNA.
DR AlphaFoldDB; G4RKU1; -.
DR STRING; 768679.TTX_1559; -.
DR PaxDb; 768679-TTX_1559; -.
DR KEGG; ttn:TTX_1559; -.
DR PATRIC; fig|768679.9.peg.1580; -.
DR eggNOG; arCOG01036; Archaea.
DR HOGENOM; CLU_035113_0_0_2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000002654; 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; IPR018214; GluRdtase_CS.
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.
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:UP000002654}.
FT DOMAIN 51..153
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 171..294
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 55..58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 111..113
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 186..191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT SITE 96
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
SQ SEQUENCE 405 AA; 44759 MW; 84C655F40E0BABE4 CRC64;
MELNQLNMPL LEKLFSASIT FREVPTEKLG ELGRSVMEML GVAPYFPIPL YVLHTCNRVE
VYAWDVPQPI VHAVLSRYGG YADRVVVRRG TEAALHLLEV AAGLDSMLIG ETDILGQMEE
AFDSQVKSHV TRDLLKVVVE RAIRFGKMVR TNTNISRGPR GLGSLSIIYV KETMGDLSNL
SIGIIGAGSV GQGLAKELKD EGARRIYILN RTFEKAKEIA ERIGATAMPL NRESIDECLK
KCDVVFATAT SFEPIIKEVP PNHKVRLIVD LGVPMNVSNN LPVKVVRLDD LKPIADRYNS
ERLQEIQKVK AMALEEVENI ERALARRAVE IELGEYMRLV ALISQEEGRR AGANASLAAN
SAAKRAVLPL IEALKKHAES GNIETVMQIL NDAKRLMKIP QASTS
//
