ID   HEM1_BACVZ              Reviewed;         455 AA.
AC   A7Z7A7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   24-JAN-2024, entry version 104.
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};
GN   OrderedLocusNames=RBAM_025230;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS74883.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000560; ABS74883.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041482263.1; NC_009725.2.
DR   AlphaFoldDB; A7Z7A7; -.
DR   SMR; A7Z7A7; -.
DR   KEGG; bay:RBAM_025230; -.
DR   HOGENOM; CLU_035113_2_2_9; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000001120; 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   NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN           1..455
FT                   /note="Glutamyl-tRNA reductase"
FT                   /id="PRO_0000335011"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         49..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         114..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         189..194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   SITE            99
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ   SEQUENCE   455 AA;  50798 MW;  A40E2CBA32BAAE6A CRC64;
     MHILVVGVDY KSAPIEIREK ISFQPDELAE AMLRLKGEKS VLENIIVSTC NRTEIYAVVD
     QLHTGRYYIK TFLSEWFSLP KEELSPFLKF YESDAAIEHL FRVACGLDSM VIGETQILGQ
     VRSSFKTAQA EKTIGTIFNE LFKQAVTVGK RTHAETDIGA NAVSVSYAAV ELAKKIFGSL
     SNKHILILGA GKMGELAAEN LHGQGIGKVT VINRTFLKAK ALADRFSGEA RSLNQLEHAL
     AEADILISST GASDFVVSKE MMERAGRQRK GRPLFMVDIA VPRDLDPALN DLEGVFLYDI
     DDLEGIVEAN LQERRETAEK VELFIEAAIV EFKQWLNTLG VVPVISALRE KALSIQSDTM
     QSIERKLPHL TVREKKLLSK HTKSIINQML RDPILKAKEL AAEADSEEKL KLFMQIFDIE
     EEAGRQLDKS LDNRQTVHSF QKAEAKTGLR PLVSE
//