ID   HEM11_CLOPH             Reviewed;         403 AA.
AC   A9KP81;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-NOV-2008, entry version 11.
DE   RecName: Full=Glutamyl-tRNA reductase 1;
DE            Short=GluTR 1;
DE            EC=1.2.1.70;
GN   Name=hemA1; OrderedLocusNames=Cphy_1368;
OS   Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=357809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H.,
RA   Brettin T., Bruce D., Detter J.C., Han C., Kuske C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-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; CP000885; ABX41743.1; -; Genomic_DNA.
DR   RefSeq; YP_001558482.1; -.
DR   GeneID; 5742318; -.
DR   GenomeReviews; CP000885_GR; Cphy_1368.
DR   KEGG; cpy:Cphy_1368; -.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP binding; 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; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   TIGRFAMs; TIGR01035; hemA; 1.
DR   PROSITE; PS00747; GLUTR; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    403       Glutamyl-tRNA reductase 1.
FT                                /FTId=PRO_0000335023.
FT   NP_BIND     183    188       NADP (By similarity).
FT   REGION       45     48       Substrate binding (By similarity).
FT   REGION      108    110       Substrate binding (By similarity).
FT   ACT_SITE     46     46       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   403 AA;  46029 MW;  497F1715C4F6418F CRC64;
     MLGIDHNKAS IEEREIFSFT KKMAADVLLN IKEIEGINGC IILSTCNRME VWVSCFEEFE
     TSIYEILCSI KKVDDNRYRH CFIERGGYDA IEHLFYMTCG LKSKIIGEDQ ILTQVREALE
     LSRENYCTDS VLETLFRFAI TSAKQVKTQI HLSVVNSSVI HHVVHELKLS NYLFKGKKCL
     VIGNGEMGKL AATKLEEEGS DVTVTVRQYR SGIIEIPVGC NRINYGDRLE HIVEYDFVIS
     ATSSPNMTIH LEQLSNLEFK KPVLFIDLAV PRDIDPRITE LKNITLYDID HFKVETVSDE
     MKTQLRQIDE ILKTKMDEFI SWYECRGIIK VVQTLSENAA IDVGLRIDKT MKKIEMDSND
     KELLAATVHS ATNKVVSKLM FGLRDHVSAA TFQECMVALK NIY
//