ID HEM1_PSEF5 Reviewed; 424 AA.
AC Q4K694;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Glutamyl-tRNA reductase;
DE Short=GluTR;
DE EC=1.2.1.70;
GN Name=hemA; OrderedLocusNames=PFL_5160;
OS Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf-5 / ATCC BAA-477;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas
RT fluorescens Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY94382.1; -; Genomic_DNA.
DR RefSeq; YP_262239.1; NC_004129.6.
DR ProteinModelPortal; Q4K694; -.
DR STRING; 220664.PFL_5160; -.
DR EnsemblBacteria; AAY94382; AAY94382; PFL_5160.
DR GeneID; 3479564; -.
DR KEGG; pfl:PFL_5160; -.
DR PATRIC; 19879783; VBIPseFlu72549_5273.
DR eggNOG; COG0373; -.
DR HOGENOM; HOG000109650; -.
DR KO; K02492; -.
DR OMA; GPILNRL; -.
DR ProtClustDB; PRK00045; -.
DR BioCyc; PFLU220664:GIX8-5201-MONOMER; -.
DR UniPathway; UPA00251; UER00316.
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 Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT CHAIN 1 424 Glutamyl-tRNA reductase.
FT /FTId=PRO_1000004672.
FT NP_BIND 187 192 NADP (By similarity).
FT REGION 49 52 Substrate binding (By similarity).
FT REGION 112 114 Substrate binding (By similarity).
FT ACT_SITE 50 50 Nucleophile (By similarity).
FT BINDING 107 107 Substrate (By similarity).
FT BINDING 118 118 Substrate (By similarity).
FT SITE 97 97 Important for activity (By similarity).
SQ SEQUENCE 424 AA; 46190 MW; 97D7A710AA2E29D6 CRC64;
MAFLALGINH KTASVDVRER VAFTPEQLVE ALQQLCRLTD SREAAILSTC NRSELYIEQD
HLSADVVLRW LAEYHHLSLD ELRASAYVHE DDAAVRHMMR VASGLDSLVL GEPQILGQMK
SAYAVAREAG TVGPLLGRLF QATFSAAKQV RTDTAIGENP VSVAFAAVSL AKQIFSDLQR
SQALLIGAGE TITLVARHLH DLGVKRIVVA NRTLERASLL AEQFGAHAVL LSDIPQELVH
SDIVISSTAS QLPILGKGAV ESALKLRKHK PIFMVDIAVP RDIEPEVGEL DDVYLYTVDD
LHEVVAENLK SRQGAAQAAE ELVNIGAEDF MVRLRELAAV DVLKAYRQQS ERLRDEELQK
ALRMLANGSG AEDVLAQLAR GLTNKLLHAP SVQLKKLSAE GRLDALAMAQ ELFALGEGSS
DKTP
//
