ID   HEM12_FLAJ1             Reviewed;         434 AA.
AC   A5FDF9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Glutamyl-tRNA reductase 2;
DE            Short=GluTR 2;
DE            EC=1.2.1.70;
GN   Name=hemA2; OrderedLocusNames=Fjoh_3752;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101)
OS   (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteria; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
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., Pitluck S., Goltsman E.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Xie G., McBride M., Richardson P.;
RT   "Complete sequence of Flavobacterium johnsoniae UW101.";
RL   Submitted (APR-2007) 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; CP000685; ABQ06765.1; -; Genomic_DNA.
DR   RefSeq; YP_001196084.1; -.
DR   GeneID; 5089786; -.
DR   GenomeReviews; CP000685_GR; Fjoh_3752.
DR   KEGG; fjo:Fjoh_3752; -.
DR   OMA; A5FDF9; EVRPEHF.
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; 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; 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    434       Glutamyl-tRNA reductase 2.
FT                                /FTId=PRO_0000335033.
FT   NP_BIND     193    198       NADP (By similarity).
FT   REGION       57     60       Substrate binding (By similarity).
FT   REGION      118    120       Substrate binding (By similarity).
FT   ACT_SITE     58     58       Nucleophile (By similarity).
FT   BINDING     113    113       Substrate (By similarity).
FT   BINDING     124    124       Substrate (By similarity).
FT   SITE        103    103       Important for activity (By similarity).
SQ   SEQUENCE   434 AA;  48167 MW;  0B3355EF5113ACFF CRC64;
     MENFNMPRST TFYALGLSYK KADAVIRGKF SLDAQAQSDL LLQAKAEGIE SLVVTSTCNR
     TEIYGFAHHP YELIKLLCEN SNGSIEEFQQ AAYIYKNEEA VSHMFRVGTG LDSQILGDFE
     IISQIKTAFN NSKQEGLVNT FLDRLVNTVI QASKKVKTET KISSGATSVS FASVQYIIRN
     VADIGSKNIL LFGTGKIGRN TCENLVKHTK NSHITLINRT KNKAELLAGK LNVIVKDYAD
     LKQELHQADV LVVATGAQNP TIDKASLALQ KPLLILDLSI PRNVDANVEE IPGVTLIHLD
     ALSQITDDTL ERRKQHIPAA EAIIDDMKLE LNTWVNGRKC APTIHALKSK LNDIVSAEFA
     FQKKKITHFD DAQMDLISSR IIQKLTNHFA SHLKNENTSV DQSIEFIEKI FQIGQLAPNK
     TSSPIADKYK INLS
//