ID   HEM1_BURCM              Reviewed;         432 AA.
AC   Q0BIP9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Bamb_0415;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
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., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
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; CP000440; ABI85974.1; -; Genomic_DNA.
DR   RefSeq; YP_772308.1; -.
DR   GeneID; 4311408; -.
DR   GenomeReviews; CP000440_GR; Bamb_0415.
DR   KEGG; bam:Bamb_0415; -.
DR   NMPDR; fig|339670.3.peg.5989; -.
DR   OMA; Q0BIP9; 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; IPR003462; ODC_Mu_crystall.
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   PANTHER; PTHR13812; ODC_Mu_crystall; 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    432       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000004599.
FT   NP_BIND     194    199       NADP (By similarity).
FT   REGION       55     58       Substrate binding (By similarity).
FT   REGION      119    121       Substrate binding (By similarity).
FT   ACT_SITE     56     56       Nucleophile (By similarity).
FT   BINDING     114    114       Substrate (By similarity).
FT   BINDING     125    125       Substrate (By similarity).
FT   SITE        104    104       Important for activity (By similarity).
SQ   SEQUENCE   432 AA;  47507 MW;  3A73F1BB532F4F57 CRC64;
     MQLLTIGINH HTAPVALRER VAFPLEQIKP ALVTFKNVFL GPHAPNAPEA AILSTCNRTE
     LYCATDDRAA REGAIRWLSE YHRISVDELA PHVYALPQSE AVRHAFRVAS GLDSMVLGET
     QILGQMKDAV RTATEAGALG TYLNQLFQRT FAVAKEVRGT TEIGAQSVSM AAAAVRLAQR
     IFETVSDQRV LFIGAGEMIE LCATHFAAQS PRELVIANRT AERGQRLAER FNGRAMPLSD
     LPTRMHEFDI IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGKLKDV
     FLYTVDDLGA IVREGNASRQ AAVAQAETII ETRVQNFMQW LDTRSVVPVI RHMHTQADAL
     RRAEVEKAQK LLARGDDPAA VLEALSQALT NKLIHGPTSA LNRVNGADRD SLIDLMRGFY
     QHAPRSNDQS GH
//