(data stored in SCRATCH zone)

HOGENOM: HALNC_1_PE1013

ID   HALNC_1_PE1013                       STANDARD;      PRT;   421 AA.
AC   HALNC_1_PE1013; D0KZK6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutamyl-tRNA reductase; Short=GluTR; EC=1.2.1 70;
DE   (HALNC_1.PE1013).
GN   Name=hemA; OrderedLocusNames=Hneap_1043;
OS   HALOTHIOBACILLUS NEAPOLITANUS C2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=555778;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HALNC_1.PE1013.
CC       Halothiobacillus neapolitanus c2, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D0KZK6_HALNC
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.
CC   -!- GENE_FAMILY: HOG000109650 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D0KZK6; -.
DR   EMBL; CP001801; ACX95879.1; -; Genomic_DNA.
DR   RefSeq; YP_003262926.1; NC_013422.1.
DR   ProteinModelPortal; D0KZK6; -.
DR   STRING; D0KZK6; -.
DR   GeneID; 8534190; -.
DR   GenomeReviews; CP001801_GR; Hneap_1043.
DR   KEGG; hna:Hneap_1043; -.
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 binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP.
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   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   SUPFAM; SSF69075; 4pyrrol_synth_GluRdtase_C; 1.
DR   SUPFAM; SSF69742; GlutR; 1.
DR   TIGRFAMs; TIGR01035; HemA; 1.
DR   PROSITE; PS00747; GLUTR; 1.
DR   HOGENOMDNA; HALNC_1.PE1013; -.
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
SQ   SEQUENCE   421 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSLIAFGLNH KTAPVDVRER IAFGPERMSS ALEGLIHGCG AKEAAIVSTC NRTEIYTRSE
     CVRENLVEWL AAFHKLPPEA IAPYVYDHRD ELAIRHLMRV ACGLDSMVLG EPQILGQIKD
     AFTIAQDAQA LGPVLSRLFQ HTFSVAKQVR TDTQIGASPV SVAFAAVSLA KQIFGDLSQK
     TALLIGAGET IELCARHLQG SGLKQVIVAN RSIDRAHHLA EQFGGLAIGL TDIPAHLHKA
     DVVISSTASP LPVLGKGAVE QALKQRKRRP IFMVDIAVPR DIEPQVSDLQ DVYLYTVDDL
     KTVIDEGQKS RAAAAEQAEE IISLQVGHFL EWVQLQTGAE LIKSYRRQSE QSRDDVLFRA
     KALLAAGKSP EETLDYLAHT LTNRLIHHPT VVLREACATG DLTAVHAVQN VLGLGGDSPS
     S
//

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