ID A0A109W7J6_9FUSO Unreviewed; 338 AA.
AC A0A109W7J6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ORFNames=AXF11_06505 {ECO:0000313|EMBL:AMD95253.1};
OS Leptotrichia sp. oral taxon 847.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1785996 {ECO:0000313|EMBL:AMD95253.1, ECO:0000313|Proteomes:UP000065271};
RN [1] {ECO:0000313|Proteomes:UP000065271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0260 {ECO:0000313|Proteomes:UP000065271};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (FEB-2016) 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; 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; CP014231; AMD95253.1; -; Genomic_DNA.
DR RefSeq; WP_068156091.1; NZ_CP014231.1.
DR AlphaFoldDB; A0A109W7J6; -.
DR STRING; 1785996.AXF11_06505; -.
DR KEGG; lot:AXF11_06505; -.
DR OrthoDB; 110209at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000065271; 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 NCBIfam; TIGR01035; hemA; 1.
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}.
FT DOMAIN 13..149
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 168..296
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 54..57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 108..110
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT BINDING 183..188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT SITE 93
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
SQ SEQUENCE 338 AA; 40013 MW; FD6065093B6F4152 CRC64;
MQNSIFCQNF FVISFSYKKM SIEERENFVK SKYKTIVENF FEKGDFLGYV IVETCLRIEI
YFETKQNFEM NNLISQFDFQ NMSFFRNEEA LIHLFDVICG LDSIIKGEDQ VLAQIKKAFF
KCLENKKTSK LLNIIFNSAI ETGKKFRNKS KINEKNMSLD SISVKFIKEK VKNIEDKTIF
IIGVGDLTQS ILTLFHKMGH KNLIVTNRSE KKSKELKKVY DNIRTAKFSQ KYEFIKKSDV
IISATSAPHL IVEYSGIKDI LRDEKERFFL DLAVPRDIDK KIAAFKNVFL YNLDDIWDLY
NQNVEKREQI VENFFYIIEE QLEKLKIKLE KQKKYSKI
//
