ID   HEM1_CHLAB              Reviewed;         338 AA.
AC   Q5L782;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, 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=CAB028;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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; CR848038; CAH63486.1; -; Genomic_DNA.
DR   RefSeq; WP_011096776.1; NC_004552.2.
DR   AlphaFoldDB; Q5L782; -.
DR   SMR; Q5L782; -.
DR   KEGG; cab:CAB028; -.
DR   eggNOG; COG0373; Bacteria.
DR   HOGENOM; CLU_035113_3_1_0; -.
DR   OrthoDB; 110209at2; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000001012; 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   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   PANTHER; PTHR43120; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43120:SF1; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF05201; GlutR_N; 1.
DR   SUPFAM; SSF69742; Glutamyl tRNA-reductase catalytic, N-terminal domain; 1.
DR   PROSITE; PS00747; GLUTR; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN           1..338
FT                   /note="Glutamyl-tRNA reductase"
FT                   /id="PRO_1000093121"
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         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         107..109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         181..186
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   SITE            92
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ   SEQUENCE   338 AA;  38300 MW;  12DEC577C95B9289 CRC64;
     MVLGVVGISY REAALKEREA VINILKDFEA NSFFSQHFFG DDGSFVLLLT CHRAEIYYFS
     KSNRHIQSKL LSRISSLGAR PYCYQGLACF THLFTVTSGM DSLISGETEI QGQVKRAYIK
     AKTDRDLPFA LHFLFQKALK EGKDFRSQVS LSHPVVTIES VVEETLDLHG KSTKDKLLFI
     GYSEINRKIA KGLSAKGYRN LIFCSRKNIS IPYDTVARSQ LSFREPYDVI FFGSSESAKD
     FSGLSLESLA SIPSRVIFDF NVPRTFTLAE SPKDIICLDM DFISERVQKK LQISKQCTNK
     EKPFLALAAR KQWEVYEKKS SHIPSSQVRA SRPKLLIL
//