ID A0A2K9LP63_9GAMM Unreviewed; 422 AA.
AC A0A2K9LP63;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=Kalk_17045 {ECO:0000313|EMBL:AUM14027.1};
OS Ketobacter alkanivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM14027.1, ECO:0000313|Proteomes:UP000235116};
RN [1] {ECO:0000313|Proteomes:UP000235116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA Kim S.-J., Rhee S.-K.;
RT "Direct submision.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP022684; AUM14027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9LP63; -.
DR KEGG; kak:Kalk_17045; -.
DR OrthoDB; 110209at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000235116; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000235116}.
FT DOMAIN 7..154
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 169..304
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 318..414
FT /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF00745"
FT COILED 298..359
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-1"
FT BINDING 49..52
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 112..114
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 187..192
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 97
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-4"
SQ SEQUENCE 422 AA; 46802 MW; E5796C7DE0326844 CRC64;
MALLAYGINH RTASVDLREK LAFSPDRVVS ALNEVRDHAR LREVAILSTC NRTELYCSAD
AENSELLLSW LGRYHALPVE NISRCVYEFW NEAAVRHLMR VASGLDSMVL GEPQILGQLK
TAYSVAQEAH TVGPELGRLF QHSFSAAKQI RTETGIGTNP VSVAFASVKL AKRIFSDLGK
TSVLLIGAGE TVELVARHLV EQGVKSITVA NRTLSRANAI AEEFKARAIT LSDIPLALPH
ADIVISSTAS PLPILGKGAV EHALKIRKHK PMFMMDIAVP RDIEEEVSEL ADVYLYTVDD
LQQVVEENRR QRKDAASKAE TLVDSCMAQF MDSLKSLDAV DAIRNYRDKL ETLRQLEMEK
ALQQIRSGTD AEVVMQRMSR SLINKVMHAP TTQLKQAAET GRNDQIEWAQ QLLGIIEPNK
PD
//
