HEM1_DICNV
ID HEM1_DICNV Reviewed; 418 AA.
AC A5EWV4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=DNO_0069;
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A;
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ13699.1; -; Genomic_DNA.
DR RefSeq; WP_011927821.1; NC_009446.1.
DR AlphaFoldDB; A5EWV4; -.
DR SMR; A5EWV4; -.
DR STRING; 246195.DNO_0069; -.
DR EnsemblBacteria; ABQ13699; ABQ13699; DNO_0069.
DR KEGG; dno:DNO_0069; -.
DR eggNOG; COG0373; Bacteria.
DR HOGENOM; CLU_035113_2_2_6; -.
DR OMA; FAFKCAA; -.
DR OrthoDB; 1358620at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000000248; 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; -; 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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 1.
DR TIGRFAMs; TIGR01035; hemA; 1.
DR PROSITE; PS00747; GLUTR; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..418
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000335028"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 51..54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 112..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 187..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 97
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ SEQUENCE 418 AA; 47667 MW; 4057163E8A12BCD8 CRC64;
MHNTIYVLGF RHQTTPASVR EKLAFSPENI LNTLPFLQAQ CAGAEILLLS TCNRSEWYFA
SNTPPRLEEW LYQHTAISSE ELKRHLFIYT DREAVQHLYR VACGLDSLIL GEPQILGQLK
AAYRLAKKAG SIGSWLERLF QHSFALAKHV RHQTDIGKNP VSVAYAGVQL THQFFDDYSK
RTAIIVGAGE TAQLVARYLH DLKIKRLIIA NRTLNRAQQL AESVGGYALS LPQLADHLHE
ADMIFGCARA DVFLVTQNMA ITALQRRQNT LQVYIDLGIP HNFDRNIDNK ENAFLYDMDN
LAQLIDKNRE TRQKAAAEAE TFIRLYSNDF LNWTQEKPQQ HMIRHIRADA HNIRQKLLIM
AYRQLAQGAD PEKVLAEMSY KLTNKLLHQP CALIHAIPPD HKDWLAVVAD TFNAELPK
