ID   HEM1_BACCN              Reviewed;         444 AA.
AC   A7GTE7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Bcer98_3182;
OS   Bacillus cereus subsp. cytotoxis (strain NVH 391-98).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA   Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H.,
RA   Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS23405.1; -; Genomic_DNA.
DR   RefSeq; YP_001376400.1; -.
DR   GeneID; 5343752; -.
DR   GenomeReviews; CP000764_GR; Bcer98_3182.
DR   KEGG; bcy:Bcer98_3182; -.
DR   OMA; A7GTE7; LLIDIAN.
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    444       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000075401.
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   444 AA;  50175 MW;  DACC1B2EC2158A6C CRC64;
     MHILVVGVNY RTVPVEIREK LTFQETELKR AMTTLQSQKS VLENVIVSTC NRTEIYAVVD
     QLHTGRYYIK KFLADWFQLE IEEISPYLSI FEQDGAIEHL FRVTCGLDSM VVGETQILGQ
     IRNSFLTAQE VKTTGTIFNE LLKQVITLAK RAHSETTIGE SAMSVSYAAV ELGKKIFGDL
     TDCHVLILGA GKMGELALQN LYGSGVQKVT VMNRTFTKAE TMAEKYMGHA KPLSELQCAL
     LEADILISST GSSNYVITKE MMKKVERMRS GRPLFMVDIA VPRDIDPEIN ELEGSFLYDI
     DDLQDVVEAN RAERLKEAEK IQFMIEEEIV LFKNWLNTLG VVPLISALRE KALGIQSETM
     RSLERKIPTL SDREKKVISK HTKSIINQLL KDPILVAKEL AAEEKATEKL ALFAKIFDLE
     VQEEVEHTEE LEHKRAWTPS VSSL
//