ID A0A0S8KWX4_9PROT Unreviewed; 366 AA.
AC A0A0S8KWX4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|RuleBase:RU000584};
DE EC=1.2.1.70 {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|RuleBase:RU000584};
DE Flags: Fragment;
GN ORFNames=AMJ72_12740 {ECO:0000313|EMBL:KPL26440.1};
OS Acidithiobacillales bacterium SM1_46.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703384 {ECO:0000313|EMBL:KPL26440.1, ECO:0000313|Proteomes:UP000052054};
RN [1] {ECO:0000313|EMBL:KPL26440.1, ECO:0000313|Proteomes:UP000052054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1_46 {ECO:0000313|EMBL:KPL26440.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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,
CC 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|RuleBase:RU000584}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000256|ARBA:ARBA00005916, ECO:0000256|RuleBase:RU000584}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPL26440.1}.
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DR EMBL; LJVB01000154; KPL26440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KWX4; -.
DR PATRIC; fig|1703384.3.peg.1101; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000052054; Unassembled WGS sequence.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-EC.
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|PIRSR:PIRSR000445-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000584};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000584}.
FT DOMAIN 1..102
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 118..252
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 266..363
FT /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF00745"
FT BINDING 135..140
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000445-3"
FT SITE 45
FT /note="Important for activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000445-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPL26440.1"
SQ SEQUENCE 366 AA; 40505 MW; 701A5A731865E0D0 CRC64;
TEVYCGLDSD GEQRIMRWFC DYHRLSLEEL RPFLYRHPDQ DAVRHAFRVA AGLDSMMLGE
TQILGQMKDA FTVAHKAGAT GKLLNRLFQQ TFSVAKQVRT DTAIGASPVS VASAAVALAK
QIFSSLASQS VLFIGAGEMI ELCARHFAEH GIGKMLVANR TLERARWLAD QFGAEAISLA
EMPNRLADAD IVVSSTASQL PILGKGAVES ALKARKHRPI LMLDIAVPRD IEPEVAELSD
VYLYAIDDLK DVVKENLESR QEAAREAEKI IDTQVSDFMH WVETLDVVPT IRALRETAEA
LCEAELKRAR RRLAAGENPE HVIEQLARAL TNKFTHSPSH ALKLANRDGN AALLEAARRL
FNLNDD
//
