ID   HEM1_ANASP              Reviewed;         428 AA.
AC   O08393;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=alr1042;
OS   Anabaena sp. (strain PCC 7120).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Woelfle M.A., Haselkorn R.;
RT   "Cloning and characterization of hemA, a gene encoding glutamyl tRNA
RT   reductase in the cyanobacterium Anabaena sp. strain 7120.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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   -!- PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis.
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; U97695; AAB58164.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB72999.1; -; Genomic_DNA.
DR   PIR; AG1936; AG1936.
DR   RefSeq; NP_485085.1; -.
DR   HSSP; Q9UXR8; 1GPJ.
DR   GeneID; 1104636; -.
DR   GenomeReviews; BA000019_GR; alr1042.
DR   KEGG; ana:alr1042; -.
DR   NMPDR; fig|103690.1.peg.1352; -.
DR   HOGENOM; O08393; -.
DR   OMA; O08393; GPILNRL.
DR   BioCyc; NSP103690:ALR1042-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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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   Chlorophyll biosynthesis; Complete proteome; NADP; Oxidoreductase;
KW   Porphyrin biosynthesis.
FT   CHAIN         1    428       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000113986.
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).
FT   CONFLICT     33     33       A -> G (in Ref. 1; AAB58164).
FT   CONFLICT     48     48       S -> G (in Ref. 1; AAB58164).
FT   CONFLICT    174    174       Q -> E (in Ref. 1; AAB58164).
FT   CONFLICT    280    280       I -> V (in Ref. 1; AAB58164).
FT   CONFLICT    374    380       DKHQEVI -> EQTSRGV (in Ref. 1; AAB58164).
SQ   SEQUENCE   428 AA;  47909 MW;  06A470955F9D3C64 CRC64;
     MNIAVVGLSH KTAPVEIREK LSIPEPQTES AIAQLTSYPH IDEVAILSTC NRLEIYIVAG
     ETDHGIREVT QFLSEHSKLP VHSLRQHLFV LLHEDAVMHI MRVAAGLDSL VLGEGQILAQ
     VKNTHKLGQQ YNGIKTILNR LFKQALTAGK RVRTETSIGT GAVSISSAAV ELAQIKAENL
     AACRVTILGA GKMSRLLVQH LVSKGATQIS IVNRSRERAQ ELAKQFSEHP IRTHLLPEMM
     TVIAESHLVF TSTSATEPIL DRAKLEMVLA PNQPLMLFDI SVPRNVHTDV NELVNVQAFN
     VDDLKAVVAQ NYESRRKMAQ EAERLLEEEI EAFDIWWRSL ETVSTISSLR SKIETIREQE
     LEKALSRLGS EFGDKHQEVI EALTRGIVNK ILHDPMVQLR AQQDVEARRR CMQTLQMLFN
     LDVGEQFS
//