ID HEM1_THEVO Reviewed; 409 AA.
AC Q97B68;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087};
DE Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087};
DE EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087};
GN Name=hemA {ECO:0000255|HAMAP-Rule:MF_00087}; OrderedLocusNames=TV0590;
GN ORFNames=TVG0579613;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00087}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00087}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00087}.
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DR EMBL; BA000011; BAB59732.1; -; Genomic_DNA.
DR PDB; 3OJ0; X-ray; 1.65 A; A=141-281.
DR PDBsum; 3OJ0; -.
DR AlphaFoldDB; Q97B68; -.
DR SMR; Q97B68; -.
DR STRING; 273116.gene:9381378; -.
DR PaxDb; 273116-14324805; -.
DR DNASU; 1441696; -.
DR KEGG; tvo:TVG0579613; -.
DR eggNOG; arCOG01036; Archaea.
DR HOGENOM; CLU_035113_2_2_2; -.
DR PhylomeDB; Q97B68; -.
DR UniPathway; UPA00251; UER00316.
DR EvolutionaryTrace; Q97B68; -.
DR Proteomes; UP000001017; 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 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 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT CHAIN 1..409
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000114113"
FT ACT_SITE 49
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 48..51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 94..96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 165..170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 79
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:3OJ0"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3OJ0"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:3OJ0"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3OJ0"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3OJ0"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:3OJ0"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:3OJ0"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3OJ0"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:3OJ0"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3OJ0"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3OJ0"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3OJ0"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3OJ0"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:3OJ0"
SQ SEQUENCE 409 AA; 46691 MW; 8CF23510B233D830 CRC64;
MLMNIVTLIS WDFKRNNESF QRAIINGYDY WSRILDDHGV EKYVILLTCN RVELYYRGDP
FDVQEKGYNI ISDDMAINHL FHVAAGLDSM SIGENEVLKQ VKQAYEKSSS MGKSDKFLSL
IFQRAISVGK LVRSKTGIGK GKVSIPSIVY DIVRKNGGNK ILLVGNGMLA SEIAPYFSYP
QYKVTVAGRN IDHVRAFAEK YEYEYVLIND IDSLIKNNDV IITATSSKTP IVEERSLMPG
KLFIDLGNPP NIERGNNVIT LDEIYEISKK NEMLREEKIN QAEILIENEM KATMNKIKDL
MIDDIFSQFY RFASVVQTME IQKFRKMHPE VNENDLEALA HSIINKILNV PVTTLKAVSR
SQGNSDFNRL FESFSSNFND IVSAALQSYE GLRDTQSLRD RTRQLLQKS
//
