ID   HEM1_ACIC1              Reviewed;         473 AA.
AC   A0LRF2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Acel_0238;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / 11B).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
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., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P.,
RA   Leu D., Pujic P., Richardson P.;
RT   "Complete sequence of Acidothermus cellulolyticus 11B.";
RL   Submitted (OCT-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; CP000481; ABK52012.1; -; Genomic_DNA.
DR   RefSeq; YP_871998.1; -.
DR   GeneID; 4485376; -.
DR   GenomeReviews; CP000481_GR; Acel_0238.
DR   KEGG; ace:Acel_0238; -.
DR   OMA; A0LRF2; 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; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    473       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000335000.
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   473 AA;  50720 MW;  BBBB567B837D1ABF CRC64;
     MSLLVVGVSH RGTPLSLLER AVLDSDQATK LLDDLVGSPV VREGMVLSTC NRVEIYACVE
     KFHPALTLIS ELLSRHGNVN FDEIAGHVHV HYDDRAVQHL FAVAAGLDSM LIGEHQVVGQ
     VRDAFRLAQE RGYAGRDLHA IVQDALHAAR RVRAETRIDS AGQTLVDVGL QILSERLGPL
     AGRRALVIGA GAMASVAVAA LTRVGITGLT VASRTLRRAT ALAQRYNGQA AALEKLADLL
     AETDVVVSCT GSVHPVVDAA TLTKAVAGRT NPLGILDIAL PHDVDPDVDR LPNVIRVDLE
     TLRPVLENTA SSADVRHARH ILDEEFDAHV ARRAAVGVVP TVVALRDKAA RVVAAELRRL
     EKRLPELDPR QFEEIRTTVH RVVDKLLHAP TVRVQELAGL AGPDSYSEAL RTLFDLDPAQ
     PVAISAPQPS TDSPARAAYQ PTDEAATDAE PRRDDAEPPS AAAAQDAGRE SRP
//