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Database: UniProt
Entry: A0A4S8KDA3_MUSBA
LinkDB: A0A4S8KDA3_MUSBA
Original site: A0A4S8KDA3_MUSBA 
ID   A0A4S8KDA3_MUSBA        Unreviewed;       548 AA.
AC   A0A4S8KDA3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   05-FEB-2025, entry version 17.
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};
GN   ORFNames=C4D60_Mb04t19680 {ECO:0000313|EMBL:THU73143.1};
OS   Musa balbisiana (Banana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=52838 {ECO:0000313|EMBL:THU73143.1, ECO:0000313|Proteomes:UP000317650};
RN   [1] {ECO:0000313|EMBL:THU73143.1, ECO:0000313|Proteomes:UP000317650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH-PKW {ECO:0000313|Proteomes:UP000317650};
RC   TISSUE=Leaves {ECO:0000313|EMBL:THU73143.1};
RA   Yao X.;
RT   "Genome sequencing of Musa balbisiana reveals subgenome evolution and
RT   function divergence in polyploid bananas.";
RL   Nat. Plants 0:0-0(2019).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). {ECO:0000256|ARBA:ARBA00002815}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate + tRNA(Glu) + NADP(+) = L-
CC         glutamyl-tRNA(Glu) + NADPH + H(+); 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:ARBA00047464,
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:THU73143.1}.
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DR   EMBL; PYDT01000001; THU73143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S8KDA3; -.
DR   STRING; 52838.A0A4S8KDA3; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000317650; Chromosome 4.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
DR   FunFam; 3.30.460.30:FF:000001; Glutamyl-tRNA reductase; 1.
DR   FunFam; 3.40.50.720:FF:000031; Glutamyl-tRNA reductase; 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; PTHR43120; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43120:SF1; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00745; GlutR_dimer; 1.
DR   Pfam; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 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   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU000584};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000584};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|RuleBase:RU000584};
KW   Reference proteome {ECO:0000313|Proteomes:UP000317650};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..548
FT                   /note="Glutamyl-tRNA reductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020198194"
FT   DOMAIN          101..251
FT                   /note="Glutamyl-tRNA reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05201"
FT   DOMAIN          268..408
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          422..527
FT                   /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00745"
SQ   SEQUENCE   548 AA;  60131 MW;  27381AAA9328A6D5 CRC64;
     MAAANSLATA FLGAAAAAAA KAEPFRANRT SNSTASPAFS FRVYQRGVAF VGSRRGAVRR
     SPRCEVQVDI KEKAAASISA IEQFKISADR YMKESSSIAV IGLSVHTAPV EMREKLAVPE
     AQWPRAVGDL CGLNHIEEAA VLSTCNRMEI YVVALSWHRG IREVTEWMSK TSGIPVSELR
     QHLFMLRDGD ATRHLFEVSG GLDSLVLGEG QILAQVKQVV RVGQVSGGLG KNIDRMFKDA
     ITTGKRVRSE TNIASGAVSV SSAAVELALM KLPKPHCGSA RMLVIGAGKM GKLVIKHLAA
     KGCKKVVVVN RSVERVEAIR EELKDIEIIY RPFSQMHACA AEADVVFTNT ASETPLFLKE
     HVQVLPTVSE DVGSVRLFVD ISVPRNVGSC VASHEHARVY NVDDLKEVVE ANKEDRLRKA
     MEAQTIITQE LKRFEAWRDS SETVPTIKNL RSYADRIRAS ELEKCLQKVG EDALTKKMRK
     AIDELSTGIV NKLLHGPLQH LRCDGSDSRT LDETLENMHA LNRMFNLQTD QKAILEQKIK
     AKVGKTQS
//
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