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A5WJM4 (A5WJM4_MYCTF) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 27. 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:TBFG_10520
OrganismMycobacterium tuberculosis (strain F11) [Complete proteome] [HAMAP]
Taxonomic identifier336982 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length468 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 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
A5WJM4 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: DDC257648FF6EAAB

FASTA46849,361
        10         20         30         40         50         60 
MSVLLFGVSH RSAPVVVLEQ LSIDESDQVK IIDRVLASPL VTEAMVLSTC NRVEVYAVVD 

        70         80         90        100        110        120 
AFHGGLSVIG QVLAEHSGMS MGELTKYAYV RYSEAAVEHL FAVASGLDSA VIGEQQVLGQ 

       130        140        150        160        170        180 
VRRAYAVAES NRTVGRVLHE LAQRALSVGK RVHSETAIDA AGASVVSVAL GMAERKLGSL 

       190        200        210        220        230        240 
AGTTAVVIGA GAMGALSAVH LTRAGVGHIQ VLNRSLSRAQ RLARRIRESG VPAEALALDR 

       250        260        270        280        290        300 
LANVLADADV VVSCTGAVRP VVSLADVHHA LAAARRDEAT RPLVICDLGM PRDVDPAVAR 

       310        320        330        340        350        360 
LPCVWVVDVD SVQHEPSAHA AAADVEAARH IVAAEVASYL VGQRMAEVTP TVTALRQRAA 

       370        380        390        400        410        420 
EVVEAELLRL DNRLPGLQSV QREEVARTVR RVVDKLLHAP TVRIKQLASA PGGDSYAEAL 

       430        440        450        460 
RELFELDQTA VDAVATAGEL PVVPSGFDAE SRRGGGDMQS SPKRSPSN

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000717 Genomic DNA. Translation: ABR04863.1.
RefSeqYP_001286465.1. NC_009565.1.

3D structure databases

ProteinModelPortalA5WJM4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5WJM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5221184.
GenomeReviewsGene locus TBFG_10520 in contig CP000717_GR.
KEGGmtf:TBFG_10520.
PATRIC18131781. VBIMycTub9078_0564.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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 nameA5WJM4_MYCTF
AccessionPrimary (citable) accession number: A5WJM4
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: December 14, 2011
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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