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Entry: A7UGU9_9FIRM
LinkDB: A7UGU9_9FIRM
Original site: A7UGU9_9FIRM 
ID   A7UGU9_9FIRM            Unreviewed;       431 AA.
AC   A7UGU9;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   13-SEP-2023, entry version 86.
DE   RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087};
DE            Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087};
DE            EC=1.2.1.70 {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087};
GN   Name=hemA2 {ECO:0000313|EMBL:ABU41507.1};
GN   Synonyms=hemA {ECO:0000256|HAMAP-Rule:MF_00087};
GN   ORFNames=EDD73_11723 {ECO:0000313|EMBL:TCP63598.1};
OS   Heliophilum fasciatum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliophilum.
OX   NCBI_TaxID=35700 {ECO:0000313|EMBL:ABU41507.1};
RN   [1] {ECO:0000313|EMBL:ABU41507.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16914272; DOI=10.1016/j.gene.2006.06.002;
RA   Guo H., Xiong J.;
RT   "A specific and versatile genome walking technique.";
RL   Gene 381:18-23(2006).
RN   [2] {ECO:0000313|EMBL:ABU41507.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17906152; DOI=10.1099/mic.0.2007/007930-0;
RA   Xiong J., Bauer C.E., Pancholy A.;
RT   "Insight into the haem d1 biosynthesis pathway in heliobacteria through
RT   bioinformatics analysis.";
RL   Microbiology 153:3548-3562(2007).
RN   [3] {ECO:0000313|EMBL:ABU41507.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xiong J.;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:TCP63598.1, ECO:0000313|Proteomes:UP000294813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11170 {ECO:0000313|EMBL:TCP63598.1,
RC   ECO:0000313|Proteomes:UP000294813};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). {ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001415, ECO:0000256|HAMAP-
CC         Rule:MF_00087, ECO:0000256|RuleBase:RU000584};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005059, ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|RuleBase:RU000584}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00087}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005916, ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|RuleBase:RU000584}.
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DR   EMBL; EU068732; ABU41507.1; -; Genomic_DNA.
DR   EMBL; SLXT01000017; TCP63598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7UGU9; -.
DR   OrthoDB; 110209at2; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000294813; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00087};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00087};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00087}; Reference proteome {ECO:0000313|Proteomes:UP000294813}.
FT   DOMAIN          6..156
FT                   /note="Glutamyl-tRNA reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05201"
FT   DOMAIN          171..306
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          321..419
FT                   /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00745"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-1"
FT   BINDING         49..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         114..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         189..194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-3"
FT   SITE            99
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-4"
SQ   SEQUENCE   431 AA;  47708 MW;  83AEE26ECAC78B25 CRC64;
     MFIFVVGLNH KSAPVEIREQ LTFSESTIGK ALDLLYSEPG ITGCAILSTC NRTEIYGSTT
     DIEKGLAAVR RFVTKMGPLA IENFANYFYT HTLYDAIRHL FRVASGLDSM VLGETQILGQ
     VRRAYQLATE HGVSNSVVNT WFQQAITVGK RVRTETGIDQ HAVSTSYTAV ELARQVFNDL
     NGKTALILGA GKMSELTLTH LIANGVSTVL VANRSFQRAE ELAGRCGGEA IHFDKLEERM
     HEADIVISCT AATHYVIRRD MVERVMATRK ERPIFFIDIA VPRDIEPSVG TVGGVHLFDI
     DDLQNVIDQN LAERSKAAAL AEVIIDQEIN DFLKWLNSLF VVPTIVALKA KGEEVRKKEL
     ERVLGRMKDL PEKDQKTISA LASSIVNQLL HDPITQIRHY AASPDGHLYS EILQNLFGLA
     ISGQRAKGKS E
//
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