ID   HEM1_ACAM1              Reviewed;         433 AA.
AC   B0BZF9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-NOV-2008, entry version 9.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=AM1_5760;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA   Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA   Mimuro M., Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW30704.1; -; Genomic_DNA.
DR   RefSeq; YP_001520023.1; -.
DR   GeneID; 5684546; -.
DR   GenomeReviews; CP000828_GR; AM1_5760.
DR   KEGG; amr:AM1_5760; -.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP binding; 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; IPR016040; NAD(P)-bd.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR13812; ODC_Mu_crystall; 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    433       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000075400.
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).
SQ   SEQUENCE   433 AA;  48281 MW;  A7BF0E37642CCEC7 CRC64;
     MNIAVVGLSH KTAPVDVREK LSIPDDVKEK ATSQLRSYPH LEEVAILSTC NRMEVYVVAQ
     ETDDGIRELT QFLSEWSQIP LLELRQHLFI LLHQDAVMHL MRVSAGLDSL VLGEGQILAQ
     VKQTHKLSQK YSGAGPILNR LFKQAISAGK RVRTETSIGT GAVSISSAAV ELAQIKTEDL
     SAHRVAIIGA GKMSRLLVKH LLSKGANQIA ILNRSLKRAE QLADQFQGAD LKLHTLADMQ
     AVLTESDLIF TSTASTEPLL DRDILEPIVC DRQSCMIFDI SVPRNVHSNV NELSQVHAFN
     VDDLKAVVAQ NQESRRQMAL EAESLLEEEV ASFDVWWRSL ETVPTISSLR TKVESIREQE
     LEKALSRLGT EFAEKHQEVI EALTRGIVNK ILHDPMVQLR AQQDIEVRRK AMQSLNMLFN
     LNSSQGVAKQ RNT
//