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Database: UniProt
Entry: A0A1U8KZP0_GOSHI
LinkDB: A0A1U8KZP0_GOSHI
Original site: A0A1U8KZP0_GOSHI 
ID   A0A1U8KZP0_GOSHI        Unreviewed;       551 AA.
AC   A0A1U8KZP0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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   Name=LOC107922393 {ECO:0000313|RefSeq:XP_016707900.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016707900.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016707900.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016707900.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_016707900.1; XM_016852411.1.
DR   AlphaFoldDB; A0A1U8KZP0; -.
DR   STRING; 3635.A0A1U8KZP0; -.
DR   PaxDb; 3635-A0A1U8KZP0; -.
DR   OrthoDB; 463at2759; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000189702; Chromosome 25.
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; 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   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:UP000189702}.
FT   DOMAIN          106..256
FT                   /note="Glutamyl-tRNA reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05201"
FT   DOMAIN          277..413
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          427..531
FT                   /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00745"
SQ   SEQUENCE   551 AA;  60411 MW;  6D1EDEE1BD9048D0 CRC64;
     MAISSTFSAA KLDSLLMNYC SSSSASFSGA YFQYQQQMKV FPRPNHGNKG MVSRNGGVRC
     EAAEFNAALG PQKIDLSKAS ALSALQQLKT SAADRYTKER SNIVVIGLSV HTAPVEMREK
     LAIPEAEMPR AIGELCGLNH IEEAAVLSTC NRMEIYVVAL SQHRGVKEVT EWMSKTSGIP
     VSKIYEHRFL LYNKDATQHL FEVSAGLDSL VLGEGQILAQ VRQVVKAGEG VLGFGRNISG
     LFKHAITVGK RVRTETNIAA GAVSVSSAAV ELAFMKLPES SHTTARMLVV GAGKMGKLVI
     KHLVAKGCTK MVVVNRSEEK VAAIREEMKG VEIIYRPFTD MLACSAEADV IFTSTASETP
     LFLKEHVKDL PPVSSEVGGL RLFIDISVPR NVGSCVTDVE GAQVYNVDDL KEVVAANKED
     RLRKAMEAQA IITEELKQFE AWRDSLETVP TIKKLRAYAD RIRLAELEKC LSKMGEDIPK
     KTRKAVDDLS RGIVNKLLHG PMQHLRCDGN DGRTLNEALE NMNALNRMFG LESDLSLVEQ
     KIRAKVEQSQ K
//
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