ID D4JBU5_9FIRM Unreviewed; 414 AA.
AC D4JBU5;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|HAMAP-Rule:MF_00087};
DE Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087};
DE EC=1.2.1.70 {ECO:0000256|HAMAP-Rule:MF_00087};
GN Name=hemA {ECO:0000256|HAMAP-Rule:MF_00087};
GN ORFNames=CC1_32770 {ECO:0000313|EMBL:CBK81816.1};
OS Coprococcus catus GD/7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81816.1, ECO:0000313|Proteomes:UP000008798};
RN [1] {ECO:0000313|EMBL:CBK81816.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81816.1,
RC ECO:0000313|Proteomes:UP000008798};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Coprococcus catus GD/7.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK81816.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81816.1,
RC ECO:0000313|Proteomes:UP000008798};
RA Pajon A.;
RL Submitted (MAR-2010) 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; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00087}.
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|HAMAP-Rule:MF_00087}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00087}.
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DR EMBL; FP929038; CBK81816.1; -; Genomic_DNA.
DR AlphaFoldDB; D4JBU5; -.
DR STRING; 717962.CC1_32770; -.
DR KEGG; cct:CC1_32770; -.
DR PATRIC; fig|717962.3.peg.3148; -.
DR HOGENOM; CLU_035113_1_0_9; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000008798; 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; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR InterPro; IPR018214; GluRdtase_CS.
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; 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; 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}.
FT DOMAIN 6..160
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 176..322
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
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 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 118..120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-2"
FT SITE 103
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT ECO:0000256|PIRSR:PIRSR000445-4"
SQ SEQUENCE 414 AA; 46814 MW; B733E31C9A59DBE7 CRC64;
MNIQLIGISH KTAPVQIRAL FAFTDENKKE LMTRICTQKE IRECVLLSTC NRTELYTVSE
ENISVRSVMT AMQRIMLDMA GIGDAGEVSE HLRFYQGTQA VRHLFYVAAG LDSMVLGEDQ
ILGQVKEAHR TAMEDGFSGT WCNSLFRMAV TAAKKVKTET KLSGISVSTA TLAVKAAEMY
FGSLENRKIL VIGATGKIGQ IMMKNIAADH YVQLYAASRQ LKSGEKAVLG TDTLSDGHGT
RHQQTEEYVQ IAYADRYRLA NEMDVIISAT ASPHYTLTKE GWQSGVIQKR RRILIDMAVP
MDIEAGIEDE ENSLCHLDEL TSLSEKNQHL RFEAADRARE MLEEDIDDFR RWALFQQNRP
LMDTFREHLL ADMAANPEKG LNKFFYRARE AADTEQLEMF FEVLRQSEEA RENG
//
