ID HEM1_SYNJB Reviewed; 431 AA.
AC Q2JJG8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 01-MAY-2013, entry version 65.
DE RecName: Full=Glutamyl-tRNA reductase;
DE Short=GluTR;
DE EC=1.2.1.70;
GN Name=hemA; OrderedLocusNames=CYB_2258;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M.,
RA Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community
RT revealed by comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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; CP000240; ABD03199.1; -; Genomic_DNA.
DR RefSeq; YP_478462.1; NC_007776.1.
DR ProteinModelPortal; Q2JJG8; -.
DR STRING; 321332.CYB_2258; -.
DR EnsemblBacteria; ABD03199; ABD03199; CYB_2258.
DR GeneID; 3900421; -.
DR KEGG; cyb:CYB_2258; -.
DR PATRIC; 23806866; VBISynSp29577_2262.
DR eggNOG; COG0373; -.
DR HOGENOM; HOG000109651; -.
DR KO; K02492; -.
DR OMA; GPILNRL; -.
DR ProtClustDB; PRK00045; -.
DR UniPathway; UPA00251; UER00316.
DR UniPathway; UPA00668; -.
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:HAMAP.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; -; 1.
DR HAMAP; MF_00087; Glu-tRNA_reductase; 1; -.
DR InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer.
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 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 SUPFAM; SSF69075; 4pyrrol_synth_GluRdtase_C; 1.
DR SUPFAM; SSF69742; GlutR; 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 1 431 Glutamyl-tRNA reductase.
FT /FTId=PRO_1000004708.
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 431 AA; 48026 MW; C34C228554FDB259 CRC64;
MFIAVVGLSH RTAPVEIRER LSIAEAEVGE TIQQLRTHPH IEEAAILSTC NRLEVYIVTS
EMESGVRQTM QFLAELKGIP LPQLRPHLFT LLYQDAVTHL MRVAAGLDSL VLGEGQILSQ
VKKAQQLGQA CNGMDRILNR LFKAAITAGK RVRTETEIGT GAMSISSAAV ELALQEQGSL
SQGKVTVVGA GRMARLLVQH LLAKGAVDIT VVNRSLERAE ALAKQFEQPI QVLPWESLLN
SVAESNLVFT STGATQPILN YQQLAGVLQP DQPLLLVDIS VPRNIDPDVE KLKGVQVFNV
DHLSRIVEEN RAQRQKLALA AEALVEEEVD QFMEWWRSLE TVPTISSLRH KVESIREQEM
EKALSRLGKD FAEKHLEVID ALTRGIVNKI LHDPMVQLRA KRDIEARRAA MRILQELFNL
DPVVFQAQQE R
//
