ID   HEM1_ALHEH              Reviewed;         446 AA.
AC   Q0AC03;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Mlg_0279;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) 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.
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DR   EMBL; CP000453; ABI55634.1; -; Genomic_DNA.
DR   RefSeq; YP_741124.1; -.
DR   GeneID; 4270497; -.
DR   GenomeReviews; CP000453_GR; Mlg_0279.
DR   KEGG; aeh:Mlg_0279; -.
DR   NMPDR; fig|187272.6.peg.263; -.
DR   HOGENOM; Q0AC03; -.
DR   OMA; Q0AC03; GPILNRL.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    446       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000004591.
FT   NP_BIND     187    192       NADP (By similarity).
FT   REGION       49     52       Substrate binding (By similarity).
FT   REGION      112    114       Substrate binding (By similarity).
FT   ACT_SITE     50     50       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   446 AA;  49827 MW;  B3DF51282454B406 CRC64;
     MSLFALGLNH KSAPVNIREQ IVFAPDAVTA ALQHLRAHTT AREAAILSTC NRTELYVRMD
     DRAPEMLGEW LARYHRLDPE WLRDYLYLHE GAGAVRHLMR VSAGLDSLVL GEPQILGQAK
     IAYQGAIDAG TMGRVLDRLF QHAFSVAKQV RTDTGIGANP VSVAFAAVTL ARQIFDDFQN
     RTALLIGAGE TIELVARHLR EQGLKNLIVA NRNLERARQL VELEGGEAIP LSEIPTRLPE
     ADVLVASTAS PLPILGKGTV ERAVRKRRHR PMFMLDLAVP RDIEPEAGNL DDVYLYTVDD
     LREVIAENRR SREEAAHQAE EIVQRQVDQF LSWRRAQQAV ASICDFRERG HAHARELLQR
     ANRRLRCGEP PERVLAWLSH TLTNRLLHAP TVGLREAAEA GDRERIELAR TLLQIENANE
     DTRESVDKEQ TGTTQGAARG DQRSTG
//