ID   HEM13_HORVU             Reviewed;         535 AA.
AC   O65796;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Glutamyl-tRNA reductase 3, chloroplastic;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Precursor;
GN   Name=HEMA3;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bonus; TISSUE=Root;
RA   Tanaka R., Yoshida K., Nakayashiki T., Tsuji H., Inokuchi H.,
RA   Okada K., Tanaka A.;
RT   "The third member of the hemA gene family encoding glutamyl-tRNA
RT   reductase is primarily expressed in roots in Hordeum vulgare.";
RL   Photosyn. Res. 53:161-171(1997).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-
CC       tRNA(Glu) to glutamate 1-semialdehyde (GSA) (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC       tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC       aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- TISSUE SPECIFICITY: Primarily expressed in roots.
CC   -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC       nucleophile attacking the alpha-carbonyl group of tRNA-bound
CC       glutamate with the formation of a thioester intermediate between
CC       enzyme and glutamate, and the concomitant release of tRNA(Glu).
CC       The thioester intermediate is finally reduced by direct hydride
CC       transfer from NADPH, to form the product GSA (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
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DR   EMBL; D88383; BAA25168.1; -; mRNA.
DR   PIR; T04402; T04402.
DR   HSSP; Q42843; 1B29.
DR   Gramene; O65796; -.
DR   BRENDA; 1.2.1.70; 283.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR   InterPro; IPR015896; 4pyrrol_synth_GluRdtase_C.
DR   InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR018214; pyrrol_synth_GluRdtase_CS.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 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   TIGRFAMs; TIGR01035; hemA; 1.
DR   PROSITE; PS00747; GLUTR; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase; Plastid;
KW   Porphyrin biosynthesis; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   CHAIN         ?    535       Glutamyl-tRNA reductase 3, chloroplastic.
FT                                /FTId=PRO_0000013312.
FT   NP_BIND     272    277       NADP (By similarity).
FT   REGION      131    133       Substrate binding (By similarity).
FT   REGION      195    197       Substrate binding (By similarity).
FT   ACT_SITE    131    131       Nucleophile (By similarity).
FT   BINDING     190    190       Substrate (By similarity).
FT   BINDING     201    201       Substrate (By similarity).
FT   SITE        180    180       Important for activity (By similarity).
SQ   SEQUENCE   535 AA;  58419 MW;  B2830889AE6A3224 CRC64;
     MASTSTASAT AMAGAFAAAG VNKPRGSAAC PRVPAGGRQR LSCVVRCDAG PGVPAQMAAM
     AASVAALEQF KISADRYMKE KSSIAVIGLS IHTAPVEMRE KLAVAEELWP RAVAELTNLN
     HIEKAAVLSP CNRMEIYVVA LSWNRGIREI VDWMSMKSGI PAVELREHLF MFRDSDATRH
     LFEVSSGLDS LVLGEGQILA QVKQVVRSGQ NSGGLGKNID RMFKDAITAG KRVRSETNIS
     CGAVSVSSAA VELALMKLPK SECLSARMLL IGAGKMGRLV AKHLAAKGCK KVVIVNRSVE
     RVDAIREEMQ GIEIVYRSLT EMYEAAADAD VVFTSTSSES PLFTKEHAEA LPPVSGALGG
     VRLFVDISVP RNVSACVSDV GHARVYNVDD LKEVVEANKE DRLRKAMEAQ TIISEELKRF
     EAWRDSMETV PTIKKLRSYA DRVRASELDK CLQKIGEDAL TKKMRRSIEQ LSTGIVNRLL
     HGPLQHLRCD GTDNRTLDET LENMHALNRM FGLDTEKAVM EQKIKTKVEK QKTQN
//