ID A0A162F7T7_9BURK Unreviewed; 443 AA.
AC A0A162F7T7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=A1D30_07990 {ECO:0000313|EMBL:KZT16790.1};
OS Acidovorax sp. GW101-3H11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT16790.1, ECO:0000313|Proteomes:UP000077219};
RN [1] {ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KZT16790.1, ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT16790.1,
RC ECO:0000313|Proteomes:UP000077219};
RX PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL Nature 557:503-509(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZT16790.1}.
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DR EMBL; LUKZ01000008; KZT16790.1; -; Genomic_DNA.
DR RefSeq; WP_063459853.1; NZ_LUKZ01000008.1.
DR AlphaFoldDB; A0A162F7T7; -.
DR STRING; 1813946.A1D30_07990; -.
DR OrthoDB; 110209at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000077219; Unassembled WGS sequence.
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 CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
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}.
FT DOMAIN 6..164
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 180..314
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 328..430
FT /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF00745"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-1"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 122..124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 197..202
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 107
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-4"
SQ SEQUENCE 443 AA; 47574 MW; 7F446D2A7269D1B9 CRC64;
MAVWALGINH TTAPLDLRGR FAFALDQIAP TLHGLRQSLG HSGGGASRHP GVETAIISTC
NRTEIYCAGD QPAMDHTLGW LAHSGGVSPA LLRSHSYTLE DSLVARHAFR VASGLDSMVL
GEAQILGQMK DAVRAAETAG ALGTTLNQLF QRSFAVAKEV RSSTEIGAHS ISMAAAAVRL
AGQLFEDLSK IRVLFVGAGE MIELCATHFA AKNPKQIAIA NRTLERGEKL ATRFGGEVMR
LADLPERLHE FDAVISCTAS SLPIIGLGAV ERALKKRRHR PMFMVDLAVP RDIEPEVKAL
GDVYLYTVDD LATVVQTAQA NRQAAVAQAE AIIDAGVQSF MHWMELRSPA AAEGGVVPLI
QQLNAQTDEW RALEIARAKK LLAKGEDVDA VLEALSRGLT QKMLHGTLAE LRAGDAEVRA
QTAQTVSRLF LRAQSKTPHN NGL
//
