ID   HEM11_PYRAR             Reviewed;         387 AA.
AC   A4WJE1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Glutamyl-tRNA reductase 1;
DE            Short=GluTR 1;
DE            EC=1.2.1.70;
GN   Name=hemA1; OrderedLocusNames=Pars_0928;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C.,
RA   Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) 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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure
CC       with each monomer consisting of three distinct domains arranged
CC       along a curved 'spinal' alpha-helix. The N-terminal catalytic
CC       domain specifically recognizes the glutamate moiety of the
CC       substrate. The second domain is the NADPH-binding domain, and the
CC       third C-terminal domain is responsible for dimerization (By
CC       similarity).
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; CP000660; ABP50508.1; -; Genomic_DNA.
DR   RefSeq; YP_001153160.1; -.
DR   GeneID; 5054302; -.
DR   GenomeReviews; CP000660_GR; Pars_0928.
DR   KEGG; pas:Pars_0928; -.
DR   OMA; A4WJE1; HTCNRVE.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00087; -; 1.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
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; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   TIGRFAMs; TIGR01035; hemA; 1.
DR   PROSITE; PS00747; GLUTR; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    387       Glutamyl-tRNA reductase 1.
FT                                /FTId=PRO_0000335096.
FT   NP_BIND     175    180       NADP (By similarity).
FT   REGION       45     48       Substrate binding (By similarity).
FT   REGION      101    103       Substrate binding (By similarity).
FT   ACT_SITE     46     46       Nucleophile (By similarity).
FT   BINDING      96     96       Substrate (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   SITE         86     86       Important for activity (By similarity).
SQ   SEQUENCE   387 AA;  43082 MW;  D8AFB667A047C5FA CRC64;
     MDLVNGLVAL SLTHKELGVD ELSKVANGVH RVCVSLRQPL FVLHTCNRVE AYLYNPPDEV
     VEIVKSGYAP YVEKVVERRG VDAARHLFRV AAGLESMLIG ETDVLGQLEE AFDRQVRAGY
     TRELLKTVVE RAIRVGKRVR TETGISRGPR GLGSLSILYV KEKIDLTNAR VCVIGAGSVG
     RGLVKELIDA GARRLVVVNR SVEKAADLGV EVWPLSERSV ERCLEDFDVV FTAVATFEPI
     IKSVPRDARV RIIVDMGMPR NTAAGLPVEV VTIDSLRDLA DRFNAMRDAE IKKAEEIVEE
     ELVALERLLR IRWVEEVSAK LLEYWFKIAE EEGERAGGLE AKIAARTTVK RTLLPVVNYL
     KKVAVSDIDE AYRIISVLRL SYGLKDL
//