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
//