(data stored in ACNUC7421 zone)

HOGENOM: SEBTE_1_PE1001

ID   SEBTE_1_PE1001                       STANDARD;      PRT;   335 AA.
AC   SEBTE_1_PE1001; D1AFK4;
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   (SEBTE_1.PE1001).
GN   Name=hemA; OrderedLocusNames=Sterm_1021;
OS   SEBALDELLA TERMITIDIS ATCC 33386.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Sebaldella.
OX   NCBI_TaxID=526218;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SEBTE_1.PE1001.
CC       Sebaldella termitidis ATCC 33386, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:D1AFK4_SEBTE
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: HOG000109108 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D1AFK4; -.
DR   EMBL; CP001739; ACZ07889.1; -; Genomic_DNA.
DR   RefSeq; YP_003307820.1; NC_013517.1.
DR   ProteinModelPortal; D1AFK4; -.
DR   GeneID; 8596500; -.
DR   GenomeReviews; CP001739_GR; Sterm_1021.
DR   KEGG; str:Sterm_1021; -.
DR   OMA; IKGEDQI; -.
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; 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; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   SUPFAM; SSF69742; GlutR; 1.
DR   TIGRFAMs; TIGR01035; HemA; 1.
DR   PROSITE; PS00747; GLUTR; 1.
DR   HOGENOMDNA; SEBTE_1.PE1001; -.
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
SQ   SEQUENCE   335 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNNMKAENFY IISFSYKSLN LEEREEFVRT GYKNIMEEYF QRKEIKGYTA LETCLRVELY
     LETGENFDID MFLERMNASN TRIYRGKDAV KYLLTVICGL DSVIKGEDQI LSQIKKTYLE
     YMENNKTSAL LNIIFNKAVE TGKKFRSVSG ISRKNLSLDS IAVKFIKSKF SNLEDKNIFI
     IGVGELSQEI LAILHKINND KITMTNRSRK KSIEVQKLFC GVMTAEFDEK YKVVKNSDII
     ISATSAPHLV LKESFMKEIL ADGKERFFLD LAVPRDIDTE LKKYNNVTLY HLEDIWDEYN
     KNIDRRNNIA DEYYYIIEEQ MEKLGKKLMS RYQRN
//

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