ID   HEM1_BORA1              Reviewed;         424 AA.
AC   Q2KZZ5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=BAV0296;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ47901.1; -; Genomic_DNA.
DR   RefSeq; YP_784834.1; -.
DR   GeneID; 6267876; -.
DR   GenomeReviews; AM167904_GR; BAV0296.
DR   KEGG; bav:BAV0296; -.
DR   NMPDR; fig|521.1.peg.1136; -.
DR   HOGENOM; Q2KZZ5; -.
DR   OMA; Q2KZZ5; 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    424       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000335012.
FT   NP_BIND     191    196       NADP (By similarity).
FT   REGION       53     56       Substrate binding (By similarity).
FT   REGION      116    118       Substrate binding (By similarity).
FT   ACT_SITE     54     54       Nucleophile (By similarity).
FT   BINDING     111    111       Substrate (By similarity).
FT   BINDING     122    122       Substrate (By similarity).
FT   SITE        101    101       Important for activity (By similarity).
SQ   SEQUENCE   424 AA;  46254 MW;  87B2847C69F13B8E CRC64;
     MSVAVLAFGL NHTSAPVSVR ERVSMPVDLV KPALAGLRSA FGGAVREAAI LSTCNRTEVY
     CAADAAVAEQ LPIWLADHHC MEAGSLHPHL YRLHQNDAVR HAFRVASGLD SMVLGEPQIL
     GQMKDAVRAA EEAGSLGTLL HQLFQRTFAV AKEVRSQTEI GAHSVSMAAA AVRLAERVFG
     DLGQARTLFI GAGEMIELCA THFAAQHPRS MVVANRTAER AESLAGRFSA GTMKLADLTE
     RLAEFDVVVS CTASSLPILG LGMVERATRQ RRHRPMVMID LAVPRDIEPE VGRLDDVYLY
     SVDDLGRLVQ SGTDARRAAV VQAEAIIETR VQGFMHWMQS REVVPVIRGL HQAAEDVQAA
     ELERARRLLA RGESPEAVLE QLAHGLTQKY LHGPLAALNR SAGDERKQLL AWMPRLFPGR
     DSRR
//