HEM1_LAWIP
ID HEM1_LAWIP Reviewed; 430 AA.
AC Q1MRJ8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=LI0322;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ54378.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM180252; CAJ54378.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041817038.1; NC_008011.1.
DR AlphaFoldDB; Q1MRJ8; -.
DR SMR; Q1MRJ8; -.
DR STRING; 363253.LI0322; -.
DR KEGG; lip:LI0322; -.
DR eggNOG; COG0373; Bacteria.
DR HOGENOM; CLU_035113_2_2_7; -.
DR OrthoDB; 1358620at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000002430; 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..430
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000335048"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 50..53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 113..115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 188..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 98
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ SEQUENCE 430 AA; 48524 MW; E184D47B6713B983 CRC64;
MEQHIYLIGM NHRTASIDVR ECFALTEHCS KDDWAIPLIK GIQESLILST CNRVEILAVG
DSNTPEIILS AWAKVKTRSI EELVPHTYTY QGRSAISHLF CVASSLDSMV LGEPQILGQL
KDAYKLATIA GASKTILNRL LHKAFSVAKR VRTETSIASN AVSISYAAVK LAKKIFGTMN
QYKAMLIGAG EMAELAAMHL MQAGIQQLKI VNRTYSQAQE LASQFRGEAI PFEKLVTYLA
EVDIVISSTG APQTIIHFND IKNILSKRKH YPMLFIDIAV PRDIDPNVHQ LDNIYLYDID
DLKEIVEDNI VQRQDEAIKA KHIIQDEIDS FCAWLQALIL QPTIVDLRKR FSTYAEEELE
RTLKKIGPVD RKTREALETM IDALIRKLTH DPISYLKCAH RTIDTNHITL ARQMFNLDKI
PQTNKAVNED
