ID   C5WWF1_SORBI            Unreviewed;       534 AA.
AC   C5WWF1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   02-SEP-2026, entry version 92.
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=SORBI_3001G202600 {ECO:0000313|EMBL:EER91419.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EER91419.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EER91419.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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}.
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DR   EMBL; CM000760; EER91419.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5WWF1; -.
DR   SMR; C5WWF1; -.
DR   STRING; 4558.C5WWF1; -.
DR   Gramene; EER91419; EER91419; SORBI_3001G202600.
DR   KEGG; sbi:8067086; -.
DR   eggNOG; ENOG502QQ1H; Eukaryota.
DR   HOGENOM; CLU_035113_2_1_1; -.
DR   InParanoid; C5WWF1; -.
DR   OMA; FAFKCAA; -.
DR   OrthoDB; 424281at2759; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000000768; Chromosome 1.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-ARBA.
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:SF19; GLUTAMYL-TRNA REDUCTASE; 1.
DR   PANTHER; PTHR43120; 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:UP000000768}.
FT   DOMAIN          88..238
FT                   /note="Glutamyl-tRNA reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05201"
FT   DOMAIN          255..395
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          409..514
FT                   /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00745"
SQ   SEQUENCE   534 AA;  58224 MW;  5FD7CD324D2347CE CRC64;
     MMASTASATA AAAAAAFGAA AKPRGSSSAP CARVAAGGRR RSGVVVRCDA GVEAQVQAVA
     KAASIAALEQ FKISADRYMK ERSSIAVIGL SVHTAPVEMR EKLAVAEELW PRAIQELTSL
     NHIEEAAVLS TCNRMEIYVV ALSWNRGIRE VVDWMSKKSG IPASELREHL FMLRDSDATR
     HLFEVSAGLD SLVLGEGQIL AQVKQVVRSG QNSGGLGKNI DRMFKDAITA GKRVRSETNI
     SSGAVSVSSA AVELALMKLP KSEALSARML LIGAGKMGKL VIKHLIAKGC KKVVVVNRSV
     ERVDAIREET KDIEIVYRPL SEMYEAAAEA DVVFTSTASE TPLFTKEHAD ALPTISDAMG
     GVRLFIDISV PRNVSACVSE IGSARVYNVD DLKEVVEANK EDRLRKAMEA QTIITEELKR
     FEAWRDSLET VPTIKKLRSY ADRIRASELE KCLQKIGDDV LTKKMRRAIE ELSTGIVNKL
     LHGPLQHLRC DGSNSRTLDE TLENMHALNR MFSLDTEKAI IEQKIKAKVE KTQN
//