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B4UAL6 (B4UAL6_ANASK) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 30. 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 2 HAMAP MF_00087
Short name=GluTR 2 HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087
Gene names
Name:hemA2 HAMAP MF_00087
Ordered Locus Names:AnaeK_1884
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length422 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 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 binding183 – 1886NADP By similarity HAMAP MF_00087
Region48 – 514Substrate binding By similarity HAMAP MF_00087
Region108 – 1103Substrate binding By similarity HAMAP MF_00087

Sites

Active site491Nucleophile By similarity HAMAP MF_00087
Binding site1031Substrate By similarity HAMAP MF_00087
Binding site1141Substrate By similarity HAMAP MF_00087
Site931Important for activity By similarity HAMAP MF_00087

Sequences

Sequence LengthMass (Da)Tools
B4UAL6 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: DAF79538EB078EDD

FASTA42244,503
        10         20         30         40         50         60 
MLVAVGLNQK GATVADREVL ALPSEELLDA LTAFQALDGV DEVAIVSTCY RVEIFAAARC 

        70         80         90        100        110        120 
PAAAELSLRH AMEARAGRPL PLFELQGEEA FRHLVRVASS LESAILGEPQ ILGQVKDAFH 

       130        140        150        160        170        180 
RAAEAGAAGK ELASVLSRAL AAAKRVRTET AVGRAGVSWG NAAAALASKV LGPLAGRRVA 

       190        200        210        220        230        240 
VIGAGEMARL TAQHMRDERA SVVVLNRTLA NAEALAAEVG GEARPLEALE QELLRADVVV 

       250        260        270        280        290        300 
SAAPAAPPAL APAVMQRILH ARRKRIVMVD LAVPRAIPAE TGALPDVYLC DVDDLDRVMK 

       310        320        330        340        350        360 
AAMAERAQAA QHAERIADEE VQKFARAEAE RRAAPLIQEM RSRASAIARE EVERTLRRLG 

       370        380        390        400        410        420 
EDPELAKRLD AMAGSIVSKI LHAPSTRLRQ AVCDGGANDP LVAAAVQIFD LSAAPAARGD 


AA

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References

[1]"Complete sequence of Anaeromyxobacter sp. K."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001131 Genomic DNA. Translation: ACG73112.1.
RefSeqYP_002134241.1. NC_011145.1.

3D structure databases

ProteinModelPortalB4UAL6.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4UAL6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6784555.
GenomeReviewsGene locus AnaeK_1884 in contig CP001131_GR.
KEGGank:AnaeK_1884.
PATRIC20938407. VBIAnaSp90767_1906.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG732626.
OMAYADIVIS.
ProtClustDBCLSK945968.

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 nameB4UAL6_ANASK
AccessionPrimary (citable) accession number: B4UAL6
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: December 14, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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