ID   HEM1_BACME              Reviewed;         446 AA.
AC   Q8GCB0;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA;
OS   Bacillus megaterium.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 509 / IFO 12109;
RX   PubMed=12408752; DOI=10.1042/BJ20021443;
RA   Raux E., Leech H.K., Beck R., Schubert H.L., Santander P.J.,
RA   Roessner C.A., Scott A.I., Martens J.H., Jahn D., Thermes C.,
RA   Rambach A., Warren M.J.;
RT   "Identification and functional analysis of enzymes required for
RT   precorrin-2 dehydrogenation and metal ion insertion in the
RT   biosynthesis of sirohaem and cobalamin in Bacillus megaterium.";
RL   Biochem. J. 370:505-516(2003).
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; AJ508220; CAD48144.1; -; Genomic_DNA.
DR   HSSP; Q9UXR8; 1GPJ.
DR   BRENDA; 1.2.1.70; 325.
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; IPR003462; ODC_Mu_crystall.
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   PANTHER; PTHR13812; ODC_Mu_crystall; 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   NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    446       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000113994.
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   446 AA;  49838 MW;  8A86F67822352A02 CRC64;
     MHIIAVGLNF RTAPVEIREK LSFNEQELAS AMKTLSGQKS ILENIIVSTC NRTEIYAVVD
     QLHTGRYYVK AFLAEWFGID KEEFSPYLTI YENDGAIEHL YRVACGLDSM VIGETQILGQ
     VRSSFLLAQE EETIGTVFNQ LFKQAVTLAK KAHHETEIGA NAVSVSYAAV ELAKKIFGDL
     SSKHVLILGA GKMGQLAVQN LYGSGAKKVT VVNRTFEKAQ ELANRFSGEA KPFADLQHAL
     SEADILISST GANDYVVTKQ MMSEAERTRK GRPLFMVDIA VPRDLDPELD ELETVFLYDI
     DDLNGIVESN LQERQKAADE IEIMLEAEIV AFKSWLGTLG VVPVISALRQ KALTIQAETM
     KSIDRKLPDL SERERKVLNK HTKSIINQLL RDPIPHAKEL AGEKHAEESL ELFMKIFNIE
     QEVALQKEKE EQLHTSITSH SVAYQS
//