Skip Header

Contribute Send feedback
Read comments (?) or add your own

B8ZT71 (B8ZT71_MYCLB) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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 EMBL CAR72520.1
Ordered Locus Names:MLBr02422
OrganismMycobacterium leprae (strain Br4923) [Complete proteome] [HAMAP]
Taxonomic identifier561304 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length467 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
B8ZT71 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: F93245F6861F96E9

FASTA46749,483
        10         20         30         40         50         60 
MSILLFGVSH RSAPVSVLEQ LSLDRSDQIK IVDRVLQSPL VTEAMVLSTC NRVEVYAVVE 

        70         80         90        100        110        120 
AFHAGLSVIG QVLSEYSAMS IGDLTKYAYV RYSEAAVEHL FTVASGLDSA VVGEQQVLGQ 

       130        140        150        160        170        180 
VRRAYAAAEA NRTVGQVLHE VAQRALSVGK RVHSETAIDA AGVSVVSVAL GIAGRTLGGL 

       190        200        210        220        230        240 
AGRIAVVIGA GAMGALSSSY LTQANVGRIH VLNRSLSRAR RLAGKIGESG VPADVWTLNH 

       250        260        270        280        290        300 
LDEALADADL VVSCTGAVSP VVSLADVHHA LAAMRRDETT RPLVICDLGM PRDVDPAVAK 

       310        320        330        340        350        360 
LPGVWVVDVE GVQREPSARA SAADVDAARR IVAAEVATYL TRQRMAEVAP TVTALRQRAA 

       370        380        390        400        410        420 
DVVEAELLRL DHRLPGLESA QREEVARTVR RVVDKLLHAP TVRIKQLASA PGGDSYTEAL 

       430        440        450        460 
RELFELDQTA VDAVATAGEL PVMVSGFSDT TRYGTSPAQS SSKYHAE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM211192 Genomic DNA. Translation: CAR72520.1.
RefSeqYP_002504197.1. NC_011896.1.

3D structure databases

ProteinModelPortalB8ZT71.
ModBaseSearch...

Protein-protein interaction databases

STRINGB8ZT71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000086063; EBMYCP00000081694; EBMYCG00000086295.
GeneID7324672.
GenomeReviewsGene locus MLBr02422 in contig FM211192_GR.
PATRIC18048955. VBIMycLep121698_4677.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000017163.
HOGENOMHBG732626.
OMAIRENEIC.
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.
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 nameB8ZT71_MYCLB
AccessionPrimary (citable) accession number: B8ZT71
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 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)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info