ID   HEM11_ANADE             Reviewed;         422 AA.
AC   Q2IJD4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Glutamyl-tRNA reductase 1;
DE            Short=GluTR 1;
DE            EC=1.2.1.70;
GN   Name=hemA1; OrderedLocusNames=Adeh_1994;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000251; ABC81764.1; -; Genomic_DNA.
DR   RefSeq; YP_465201.1; -.
DR   GeneID; 3887141; -.
DR   GenomeReviews; CP000251_GR; Adeh_1994.
DR   KEGG; ade:Adeh_1994; -.
DR   HOGENOM; Q2IJD4; -.
DR   OMA; Q2IJD4; IICATSS.
DR   BioCyc; ADEH290397:ADEH_1994-MON; -.
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    422       Glutamyl-tRNA reductase 1.
FT                                /FTId=PRO_0000335005.
FT   NP_BIND     183    188       NADP (By similarity).
FT   REGION       48     51       Substrate binding (By similarity).
FT   REGION      108    110       Substrate binding (By similarity).
FT   ACT_SITE     49     49       Nucleophile (By similarity).
FT   BINDING     103    103       Substrate (By similarity).
FT   BINDING     114    114       Substrate (By similarity).
FT   SITE         93     93       Important for activity (By similarity).
SQ   SEQUENCE   422 AA;  44435 MW;  B2F7050D3958C325 CRC64;
     MLVAVGLNQK GATVADREVL ALPSEELLDA LTAFQALDGV DEVAIVSTCY RVEIFAAARC
     PAAAELSLRH ALEARAGRSL PLFELQGEEA FRHLVRVASS LESAILGEPQ ILGQVKDAFH
     RAAEAGAAGK ELASVLSRAL AAAKRVRTET AVGRAGVSWG NAAAALASKV LGPLAGRRVA
     VIGAGEMARL TAQHMRDERA SVVVLNRTLA NAEALAAEVG GEARPLDALE QELLRADVVV
     SAAPAAPAAL APAVMQRILH ARRKRIVMVD LAVPRAIPAE TGALPDVYLC DVDDLDRVMK
     AAMAERAQAA QHAERIADEE VQKFARAEAE RRAAPLIQEM RSRASAIARE EVERTLRRLG
     EDPELAKRLD AMAGSIVSKI LHAPSTRLRQ AVCDGGANDP LVAAAVQIFD LSAAPAARGD
     AA
//