ID   HEM12_ARATH             Reviewed;         530 AA.
AC   P49294; O04950; Q0WQP1; Q4V3B7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   16-DEC-2008, entry version 72.
DE   RecName: Full=Glutamyl-tRNA reductase 2, chloroplastic;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Precursor;
GN   Name=HEMA2; OrderedLocusNames=At1g09940; ORFNames=F21M12.33;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=96189258; PubMed=8605295; DOI=10.1007/BF00049321;
RA   Kumar A.M., Csankovszki G., Soell D.;
RT   "A second and differentially expressed glutamyl-tRNA reductase gene
RT   from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 30:419-426(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in low levels in roots and flowers.
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; U27118; AAB01674.1; -; Genomic_DNA.
DR   EMBL; AC000132; AAB60749.1; -; Genomic_DNA.
DR   EMBL; BT023439; AAY56430.1; -; mRNA.
DR   EMBL; AK228651; BAF00558.1; -; mRNA.
DR   PIR; G86233; G86233.
DR   PIR; S65773; S65773.
DR   RefSeq; NP_172465.1; -.
DR   UniGene; At.27711; -.
DR   HSSP; Q9UXR8; 1GPJ.
DR   GeneID; 837528; -.
DR   GenomeReviews; CT485782_GR; AT1G09940.
DR   KEGG; ath:AT1G09940; -.
DR   NMPDR; fig|3702.1.peg.1230; -.
DR   TAIR; At1g09940; -.
DR   BioCyc; MetaCyc:AT1G09940-MON; -.
DR   ArrayExpress; P49294; -.
DR   GermOnline; AT1G09940; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP 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:0006783; P:heme biosynthetic process; IEP:TAIR.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR   InterPro; IPR015896; 4pyrrol_synth_GluRdtase_C.
DR   InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR   InterPro; IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
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; Complete proteome; NADP;
KW   Oxidoreductase; Plastid; Porphyrin biosynthesis; Transit peptide.
FT   TRANSIT       1     64       Chloroplast (Potential).
FT   CHAIN        65    530       Glutamyl-tRNA reductase 2, chloroplastic.
FT                                /FTId=PRO_0000013308.
FT   NP_BIND     277    282       NADP (By similarity).
FT   REGION      134    137       Substrate binding (By similarity).
FT   REGION      199    201       Substrate binding (By similarity).
FT   ACT_SITE    135    135       Nucleophile (By similarity).
FT   BINDING     194    194       Substrate (By similarity).
FT   BINDING     205    205       Substrate (By similarity).
FT   SITE        184    184       Important for activity (By similarity).
FT   CONFLICT    245    245       A -> G (in Ref. 4; BAF00558).
FT   CONFLICT    410    410       D -> E (in Ref. 1; AAB01674).
SQ   SEQUENCE   530 AA;  58292 MW;  0C0224296BA3D0A8 CRC64;
     MAVSSAFVVT PKLEKLLANH HNPTYSSSPA PLDVIGIRAL PMNNRNKRGL IQRARCEISP
     SNKAASISAL EQLKTSAIDR YTKERSSIVV IGLSIHTAPV EMREKLAIPE AEWPRAIAEL
     CGLNHIEEAA VLSTCNRMEI YVLALSQHRG VKEVTEWMSK TSGIPVSEIC QHRFLLYNKD
     VTQHIFEVSA GLDSLVLGEG QILAQVKQVV KVGQGVNGFG RNISGLFKHA ITVGKRVRTE
     TNIAAGAVSV SSAAVELALM KLPESSHASS ARMLVVGAGK MGKLVIKHLV AKGCTKMVVV
     NRSEEKVAAV RNEMPPGVEI IYKPLDEMLS CAAEADVVFT STASETPLFL KEQVETLPPV
     RDARLFVDIS VPRNVGSCVA EIDGTRVFNV DDLKEVVAAN KEDRVRKAMD AQAIITDESK
     HFEAWRDSLE TVPTIKKLRG YTERIIAAEI EKSLPKMGID MNKKMRKTVD DLIRGIVNKL
     LHGPMQHLRC DGNDSRTLSE TLDNMQALNR MYGLDAEILE EKIRAKVEKK
//