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Database: UniProt
Entry: A0A021VNH2_9CELL
LinkDB: A0A021VNH2_9CELL
Original site: A0A021VNH2_9CELL 
ID   A0A021VNH2_9CELL        Unreviewed;       407 AA.
AC   A0A021VNH2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=glutamyl-tRNA reductase {ECO:0000256|ARBA:ARBA00012970};
DE            EC=1.2.1.70 {ECO:0000256|ARBA:ARBA00012970};
DE   Flags: Fragment;
GN   ORFNames=N866_06455 {ECO:0000313|EMBL:EYR62653.1};
OS   Actinotalea ferrariae CF5-4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Actinotalea.
OX   NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR62653.1, ECO:0000313|Proteomes:UP000019753};
RN   [1] {ECO:0000313|EMBL:EYR62653.1, ECO:0000313|Proteomes:UP000019753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF5-4 {ECO:0000313|EMBL:EYR62653.1,
RC   ECO:0000313|Proteomes:UP000019753};
RA   Chen F., Li Y., Wang G.;
RT   "Actinotalea ferrariae CF5-4.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005059}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005916}.
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:EYR62653.1}.
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DR   EMBL; AXCW01000196; EYR62653.1; -; Genomic_DNA.
DR   RefSeq; WP_052023085.1; NZ_AXCW01000196.1.
DR   AlphaFoldDB; A0A021VNH2; -.
DR   OrthoDB; 110209at2; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000019753; 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   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   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   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019753}.
FT   DOMAIN          17..108
FT                   /note="Glutamyl-tRNA reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05201"
FT   DOMAIN          128..256
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          274..366
FT                   /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00745"
FT   REGION          376..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141..146
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000445-3"
FT   SITE            52
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000445-4"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EYR62653.1"
SQ   SEQUENCE   407 AA;  41408 MW;  1976F066A3FEF263 CRC64;
     PAAESLADRA HRAAIADAAR DVVAVVARTS GLDATAVTES LQLAVGPAVS RHLFAVGAGL
     DSMVVGEREV AGQVRRALQT ARGLGTTSST LERLFQSASR ASRAVGSGTA LGGTGRSVVG
     VALDLVAQDV DLRQASVLLI GTGSYAGASL TALRTRGARD VAVYSPSGRA HGFATDRGAR
     PVEAGDLPGA LAAADVVVSC SGALGPVVDV PMVTAARAAD PTGTPRPRVL VDLALTHDVD
     PAVATVPGVR LVDLATIQAH APAAVSREVT RGRRIVEEHA AEFEATLAEQ TLVPAVVALR
     RHVEQAMAAE LHRVRAGDPE VAAAVERSLR RFAASVLHVP AVRAREHARR GRHDEYREGL
     EAVFGLQVQA GALTGAGALT AGGPDGLDDA GDPDDDAPHG PPPAASA
//
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