ID   HEM1_AQUAE              Reviewed;         406 AA.
AC   O67314;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=aq_1279;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07274.1; -; Genomic_DNA.
DR   PIR; G70410; G70410.
DR   RefSeq; NP_213878.1; -.
DR   HSSP; Q9UXR8; 1GPJ.
DR   GeneID; 1192752; -.
DR   GenomeReviews; AE000657_GR; aq_1279.
DR   KEGG; aae:aq_1279; -.
DR   NMPDR; fig|224324.1.peg.893; -.
DR   HOGENOM; O67314; -.
DR   OMA; O67314; GPILNRL.
DR   BioCyc; AAEO224324:AQ_1279-MON; -.
DR   BRENDA; 1.2.1.70; 189781.
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   PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 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    406       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000113987.
FT   NP_BIND     187    192       NADP (By similarity).
FT   REGION       50     53       Substrate binding (By similarity).
FT   REGION      112    114       Substrate binding (By similarity).
FT   ACT_SITE     51     51       Nucleophile (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     118    118       Substrate (By similarity).
FT   SITE         97     97       Important for activity (By similarity).
SQ   SEQUENCE   406 AA;  46648 MW;  77F3ECC488FC4394 CRC64;
     MGEIFVAGVN FKVAPVEVRE KLACSLEETK KVLPILKRET PLEEVMLLST CNRVEVYAYN
     FVENSEDLIN KLLEIKRLNP SFKRYFFVKR GEEAVYHIFK VASSLDSMVI GEPQIVAQFK
     EAYRVAKEAG TVGKILNRVY EKALRASKRV RTETGISRSA VSVSYAAVEL AKKIFGDLKE
     AKVLLIGAGE MGELAANYLR RFGAKLHITN RTYERALKLV KELSGNVLRF EELKEYLPLM
     DIVIVSTGAK DYILKREDFE RSVRERHYEP QFVIDIAVPR NVDPEAGNVE GVFLYDIDDL
     KQVVEENLKE RIKEAQRGEI ILWDEVKKFM NWYESLKAEP YILELKASVE GKEVSPYIKK
     LVHRAIKEIK RNPEVADIIL RIFKEVEKNE PRRKELSNVY NGTHGA
//