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HEM1_CHLT3
ID   HEM1_CHLT3              Reviewed;         437 AA.
AC   B3QWI0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Ctha_2289;
OS   Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chloroherpeton.
OX   NCBI_TaxID=517418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35110 / GB-78;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL   Submitted (JUN-2008) 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   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis. {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; CP001100; ACF14740.1; -; Genomic_DNA.
DR   RefSeq; WP_012500823.1; NC_011026.1.
DR   AlphaFoldDB; B3QWI0; -.
DR   SMR; B3QWI0; -.
DR   STRING; 517418.Ctha_2289; -.
DR   PRIDE; B3QWI0; -.
DR   EnsemblBacteria; ACF14740; ACF14740; Ctha_2289.
DR   KEGG; cts:Ctha_2289; -.
DR   eggNOG; COG0373; Bacteria.
DR   HOGENOM; CLU_035113_2_2_10; -.
DR   OMA; FAFKCAA; -.
DR   OrthoDB; 1358620at2; -.
DR   UniPathway; UPA00251; UER00316.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000001208; 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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
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   Chlorophyll biosynthesis; NADP; Oxidoreductase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..437
FT                   /note="Glutamyl-tRNA reductase"
FT                   /id="PRO_1000093125"
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   437 AA;  49497 MW;  20C5230775AC0FBB CRC64;
     MNLIAVGVNH NTAPIELREK ISLTDSMARS LLTELIDSKL ASEALVLSTC NRTELYVVPA
     MPEVTANYLK DYLIAHKGVR KEVTRDHFFN YFACGAARHF YNVACAIDSL ILGEVQIIGQ
     VKTAYNRAVE MKTVGPILNK MCHTGFGLAN RVRSKTKLTA GAVSVSYAAV ELTQKIYSDV
     STKNILLVGA GDTAKLAAKN LLDKRVRDFY ITNRTYEKAE LLAQELGTGK ILPLEEMTER
     LHEFDIVVTA VGGNDHIIKK EHVAAAMQKR HRDPILILDL GLPRNVAPEV GQVNNVFLKD
     IDDLKMIIDS NLEKRRAEIP KVKHFIQKEL IEYARWYFSL EVKPTIVDLQ EKFFEIKALE
     LARIKNKVSA EEYERMEQLS DRIIKKLLHF PITTLKQQTA DTTDPVSFIR NIFDLKEQEE
     EFPGLTFPIN LKEQNNN
 
 
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