MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087}; Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087}; EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087}; |
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| MyHits synonyms | HEM1_SHIF8 , Q0T5I5 , E756E4F2928C535A |
 Legends: 1, ACT_SITE Nucleophile. {ECO:0000255|HAMAP- Rule:MF_00087}; 2, BINDING Substrate. {ECO:0000255|HAMAP- Rule:MF_00087}; 3, SITE Important for activity. {ECO:0000255|HAMAP-Rule:MF_00087}; 4, NP_BIND NADP. {ECO:0000255|HAMAP-Rule:MF_00087}; 5, REGION Substrate binding. {ECO:0000255|HAMAP- Rule:MF_00087}; 6, ipat:GLUTR [T].
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ID HEM1_SHIF8 Reviewed; 418 AA.
AC Q0T5I5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 02-NOV-2016, entry version 78.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087};
DE Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087};
DE EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087};
GN Name=hemA {ECO:0000255|HAMAP-Rule:MF_00087};
GN OrderedLocusNames=SFV_1224;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-
CC tRNA(Glu) to glutamate 1-semialdehyde (GSA). {ECO:0000255|HAMAP-
CC Rule:MF_00087}.
CC -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. {ECO:0000255|HAMAP-
CC Rule:MF_00087}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC 1/2. {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00087}.
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.
CC {ECO:0000255|HAMAP-Rule:MF_00087}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00087}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF03430.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR EMBL; CP000266; ABF03430.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005049668.1; NC_008258.1.
DR ProteinModelPortal; Q0T5I5; -.
DR EnsemblBacteria; ABF03430; ABF03430; SFV_1224.
DR KEGG; sfv:SFV_1224; -.
DR PATRIC; 18725770; VBIShiFle33408_1409.
DR HOGENOM; HOG000109650; -.
DR KO; K02492; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000000659; Chromosome.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; IPR018214; GluRdtase_CS.
DR InterPro; IPR016040; NAD(P)-bd_dom.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 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 1 418 Glutamyl-tRNA reductase.
FT /FTId=PRO_0000335072.
FT NP_BIND 189 194 NADP. {ECO:0000255|HAMAP-Rule:MF_00087}.
FT REGION 49 52 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00087}.
FT REGION 114 116 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00087}.
FT ACT_SITE 50 50 Nucleophile. {ECO:0000255|HAMAP-
FT Rule:MF_00087}.
FT BINDING 109 109 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00087}.
FT BINDING 120 120 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00087}.
FT SITE 99 99 Important for activity.
FT {ECO:0000255|HAMAP-Rule:MF_00087}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 6 156 ipfam:GlutR_N [T]
FT MYHIT 99 122 ipat:GLUTR [T]
FT MYHIT 172 306 ipfam:Shikimate_DH [T]
FT MYHIT 2 418 ihamap:Glu_tRNA_reductase [T]
FT MYHIT 320 416 ipfam:GlutR_dimer [T]
SQ SEQUENCE 418 AA; 46358 MW; E756E4F2928C535A CRC64;
MTLLALGINH KTAPVSLRER VSFSPDKLDQ ALDSLLAQPM VQGGVVLSTC NRTELYLSVE
EQDNLQEALI RWLCDYHNLN EEDLRKSLYW HQDNDAVSHL MRVASGLDSL VLGEPQILGQ
VKKAFVDSQK GHMKASELER MFQKSFSVAK RVRTETDIGA SAVSVAFAAC TLARQIFESL
STVTVLLVGA GETIELVARH LREHKVQKMI IANRTRERAQ ILADEVGAEV IALSEIDERL
READIIISST ASPLPIIGKG MVERALKSRR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV
DDLQSIISHN LAQRKAAAVE AETIVAQETS EFMAWLRAQS ASETIREYRS QAEHVRDELT
AKALAALEQG GDAQAIMQDL AWKLTNRLIH APTKSLQQAA RDGDNERLNI LRDSLGLE
//
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