ID   HEM1_BACA2              Reviewed;         455 AA.
AC   A7Z7A7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=RBAM_025230;
OS   Bacillus amyloliquefaciens (strain FZB42).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant
RT   growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS74883.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001422114.1; -.
DR   GeneID; 5460787; -.
DR   GenomeReviews; CP000560_GR; RBAM_025230.
DR   KEGG; bay:RBAM_025230; -.
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; 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   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    455       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000335011.
FT   NP_BIND     189    194       NADP (By similarity).
FT   REGION       49     52       Substrate binding (By similarity).
FT   REGION      114    116       Substrate binding (By similarity).
FT   ACT_SITE     50     50       Nucleophile (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   BINDING     120    120       Substrate (By similarity).
FT   SITE         99     99       Important for activity (By similarity).
SQ   SEQUENCE   455 AA;  50798 MW;  A40E2CBA32BAAE6A CRC64;
     MHILVVGVDY KSAPIEIREK ISFQPDELAE AMLRLKGEKS VLENIIVSTC NRTEIYAVVD
     QLHTGRYYIK TFLSEWFSLP KEELSPFLKF YESDAAIEHL FRVACGLDSM VIGETQILGQ
     VRSSFKTAQA EKTIGTIFNE LFKQAVTVGK RTHAETDIGA NAVSVSYAAV ELAKKIFGSL
     SNKHILILGA GKMGELAAEN LHGQGIGKVT VINRTFLKAK ALADRFSGEA RSLNQLEHAL
     AEADILISST GASDFVVSKE MMERAGRQRK GRPLFMVDIA VPRDLDPALN DLEGVFLYDI
     DDLEGIVEAN LQERRETAEK VELFIEAAIV EFKQWLNTLG VVPVISALRE KALSIQSDTM
     QSIERKLPHL TVREKKLLSK HTKSIINQML RDPILKAKEL AAEADSEEKL KLFMQIFDIE
     EEAGRQLDKS LDNRQTVHSF QKAEAKTGLR PLVSE
//