(data stored in ACNUC7421 zone)

HOGENOM: SALPK_1_PE1015

ID   SALPK_1_PE1015                       STANDARD;      PRT;   418 AA.
AC   SALPK_1_PE1015; B5BI74;
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   (SALPK_1.PE1015).
GN   Name=hemA; OrderedLocusNames=SSPA1023;
OS   SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR PARATYPHI A STR. AKU_12601.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SALPK_1.PE1015.
CC       Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601
CC       chromosome, complete genome.
CC   -!- ANNOTATIONS ORIGIN:HEM1_SALPK
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; B5BI74; -.
DR   EMBL; FM200053; CAR59176.1; -; Genomic_DNA.
DR   RefSeq; YP_002141864.1; NC_011147.1.
DR   ProteinModelPortal; B5BI74; -.
DR   STRING; B5BI74; -.
DR   PRIDE; B5BI74; -.
DR   GeneID; 6810310; -.
DR   GenomeReviews; FM200053_GR; SSPA1023.
DR   KEGG; sek:SSPA1023; -.
DR   OMA; GPILNRL; -.
DR   ProtClustDB; PRK00045; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:EC.
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:UniProtKB-KW.
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; SALPK_1.PE1015; -.
KW   glutamyl-tRNA reductase;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
SQ   SEQUENCE   418 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTLLALGINH KTAPVSLRER VTFSPDTLDQ ALDSLLAQPM VQGGVVLSTC NRTELYLSVE
     EQDNLQEALI RWLCDYHNLN EDDLRNSLYW HQDNDAVSHL MRVASGLDSL VLGEPQILGQ
     VKKAFADSQK GHLNASALER MFQKSFSVAK RVRTETDIGA SAVSVAFAAC TLARQIFESL
     STVTVLLVGA GETIELVARH LREHKVQKMI IANRTRERAQ ALADEVGAEV ISLSDIDARL
     QDADIIISST ASPLPIIGKG MVERALKSRR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV
     DDLQSIISHN LAQRQAAAVE AETIVEQEAS EFMAWLRAQG ASETIREYRS QSEQIRDELT
     TKALSALQQG GDAQAILQDL AWKLTNRLIH APTKSLQQAA RDGDDERLNI LRDSLGLE
//

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