ID   HEM12_PYRAR             Reviewed;         403 AA.
AC   A4WN38;
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 2;
DE            Short=GluTR 2;
DE            EC=1.2.1.70;
GN   Name=hemA2; OrderedLocusNames=Pars_2261;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000660; ABP51805.1; -; Genomic_DNA.
DR   RefSeq; YP_001154457.1; -.
DR   GeneID; 5055414; -.
DR   GenomeReviews; CP000660_GR; Pars_2261.
DR   KEGG; pas:Pars_2261; -.
DR   OMA; A4WN38; VDLGVPQ.
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    403       Glutamyl-tRNA reductase 2.
FT                                /FTId=PRO_0000335097.
FT   NP_BIND     177    182       NADP (By similarity).
FT   REGION       47     50       Substrate binding (By similarity).
FT   REGION      103    105       Substrate binding (By similarity).
FT   ACT_SITE     48     48       Nucleophile (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   SITE         88     88       Important for activity (By similarity).
SQ   SEQUENCE   403 AA;  43952 MW;  67ACEFEC46ADA556 CRC64;
     MDLLSPLSAV ILTYREADAN ALGRIGEEMR RCIEVIGPKT PMFVLHTCHR VEAYLYGASE
     EELSSLVERY KRHVESARIL RGIEAARHLF RVAAGLESML LGETDILGQL EEAYDRQVRA
     GFTRGLLKTV VERAVRVGKK VRTETGISRG PAGLGSLSII YVSQFVDLKS AKVAVLGAGA
     VGAGLAKELA ERGVAKLYIL NRTLEKATEV AKKTGAEARP LTREEVERCL LECDVVFSAV
     HTLEYVIDMI PPGASVKVVV DLGVPQSVAP GLPIKVVRLS DLAELAQRYS ALRKEEAKKA
     EAIVEEELEM LPKALAKRAV EEAVAEVMAR AVEIAEEEGR RAGCEVAQLA AKTTVKRLLL
     PIVEELKKMA ENGRVEHALE VSQIFTRLVG APHGEPQNLK TVK
//