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B0TBK9 (B0TBK9_HELMI) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase 1 HAMAP MF_00087
Short name=GluTR 1 HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087
Gene names
Name:hemA EMBL ABZ83848.1
Synonyms:hemA1 HAMAP MF_00087
Ordered Locus Names:Helmi_12230
ORF Names:HM1_0704 EMBL ABZ83848.1
OrganismHeliobacterium modesticaldum (strain ATCC 51547 / Ice1) [Complete proteome] [HAMAP]
Taxonomic identifier498761 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Heliobacteriaceae › Heliobacterium

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP MF_00087 SAAS SAAS018214

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214

Pathway

Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP MF_00087

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214

Subunit structure

Homodimer By similarity. HAMAP MF_00087 SAAS SAAS018214

Domain

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity. HAMAP MF_00087

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity. HAMAP MF_00087

Sequence similarities

Belongs to the glutamyl-tRNA reductase family. HAMAP MF_00087 RuleBase RU000584

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding189 – 1946NADP By similarity HAMAP MF_00087
Region49 – 524Substrate binding By similarity HAMAP MF_00087
Region114 – 1163Substrate binding By similarity HAMAP MF_00087

Sites

Active site501Nucleophile By similarity HAMAP MF_00087
Binding site1091Substrate By similarity HAMAP MF_00087
Binding site1201Substrate By similarity HAMAP MF_00087
Site991Important for activity By similarity HAMAP MF_00087

Sequences

Sequence LengthMass (Da)Tools
B0TBK9 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: A07524366A0D9889

FASTA44549,357
        10         20         30         40         50         60 
MFIFAVGLNH KSAPVEVREK LSFTEAQISE ALTQLEGMTG IEGCCILATC NRTEIYGACT 

        70         80         90        100        110        120 
DLEAGLAAVK RFIIERGRLQ PSDFANYFYV HTLYDAIRHL FRVASGLDSM VLGETQILGQ 

       130        140        150        160        170        180 
VRAAYQRACN ERASNGIINT LFQQAITVGK RVRSETGIDQ HPVSISYTAV ELAEQVFGGL 

       190        200        210        220        230        240 
AGRSAMVLGA GKMSVLTLKH LVAQGVERII IANRSVEKAK ELAQGCGGEA IPFHEVHARM 

       250        260        270        280        290        300 
AEADIVISCT AATHYVIRRP MMEEVMERRS GKPVFLIDIA VPRDIDPEVA QVSGVHLYDI 

       310        320        330        340        350        360 
DDLQHVVDRN LEERRKAAIE AEEIIESEIT QFLRWLNSLF VIPTIVSLKQ KGNQIREKEL 

       370        380        390        400        410        420 
GRALSKLKHL SEKEKKLVGS LASSIVNQLL HDPITRLRHY AATPEGHLYS EILQNLFCLD 

       430        440 
VPGQRQKHAA PRLHVVESSR QNHGG

« Hide

References

[1]"The genome of Heliobacterium modesticaldum, a phototrophic representative of the Firmicutes containing the simplest photosynthetic apparatus."
Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M., Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.
J. Bacteriol. 190:4687-4696(2008) [PubMed: 18441057] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000930 Genomic DNA. Translation: ABZ83848.1.
RefSeqYP_001679859.1. NC_010337.2.

3D structure databases

ProteinModelPortalB0TBK9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0TBK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5911642.
GenomeReviewsGene locus Helmi_12230 in contig CP000930_GR.
KEGGhmo:HM1_0704.
PATRIC22106709. VBIHelMod36755_1134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG732626.
OMAPESSHAT.
ProtClustDBPRK00045.

Family and domain databases

HAMAPMF_00087. Glu_tRNA_reductase.
[Tree]
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK02492.
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit.
SSF69742. GlutR. 1 hit.
TIGRFAMsTIGR01035. HemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB0TBK9_HELMI
AccessionPrimary (citable) accession number: B0TBK9
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info