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B8GJJ4 (B8GJJ4_METPE) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. 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 HAMAP MF_00087

Short name=GluTR HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087
Gene names
Name:hemA HAMAP MF_00087
Ordered Locus Names:Mpal_1728
OrganismMethanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c) [Complete proteome] [HAMAP]
Taxonomic identifier521011 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesGenera incertae sedisMethanosphaerula

Protein attributes

Sequence length425 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

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP MF_00087

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 binding180 – 1856NADP By similarity HAMAP MF_00087
Region52 – 554Substrate binding By similarity HAMAP MF_00087
Region105 – 1073Substrate binding By similarity HAMAP MF_00087

Sites

Active site531Nucleophile By similarity HAMAP MF_00087
Binding site1001Substrate By similarity HAMAP MF_00087
Binding site1111Substrate By similarity HAMAP MF_00087
Site901Important for activity By similarity HAMAP MF_00087

Sequences

Sequence LengthMass (Da)Tools
B8GJJ4 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: BB53CECED71571F3

FASTA42546,559
        10         20         30         40         50         60 
MAVDPLFAHI AIGGMNHHTA DMDMLEQFRF GDEEQFLADI QVHFKGAILL QTCNRVEILV 

        70         80         90        100        110        120 
QGTGAGLTEY LHELGRASFE VREDLDAIRH LLEVACGIDS MIVGEDQILG QLKKALAAAQ 

       130        140        150        160        170        180 
TAGACSPLIE QCVNKAVHVG VEVRRRTEIN RGAVSIGSAA VTLAEELLGT LTGRHILVVG 

       190        200        210        220        230        240 
GGEIGMLVTQ ALAAKDLTAI YVANRTYARA VQLASKIGGK AVTMAEMHRY LVLSDVVISC 

       250        260        270        280        290        300 
TSAPHPIIRC EELKEVMKGR CWPLEGHPRP LILIDIAQPR DVEVGADQID GVHLCTIDNL 

       310        320        330        340        350        360 
RTISQNNLDY RKSEASRAQT YIEEELNQFV QLINRKAADD HLSMLHSWAE QIRVRERDRA 

       370        380        390        400        410        420 
LARLGSEDQR AVAVVDDLTR VLVKKLLTDA TFSIRASAEC GEMEAAASLV HAITQGEKLC 


IQKKE 

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References

[1]"Complete sequence of Candidatus Methanosphaerula E1-9c."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Lu M., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.O., Zinder S.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1556 / DSM 19958 / E1-9c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001338 Genomic DNA. Translation: ACL17035.1.
RefSeqYP_002466758.1. NC_011832.1.

3D structure databases

ProteinModelPortalB8GJJ4.
ModBaseSearch...

Protein-protein interaction databases

STRINGB8GJJ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7271291.
GenomeReviewsGene locus Mpal_1728 in contig CP001338_GR.
KEGGmpl:Mpal_1728.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG732626.
OMAGPILNRL.
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 nameB8GJJ4_METPE
AccessionPrimary (citable) accession number: B8GJJ4
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: December 14, 2011
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)