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B2HRJ1 (B2HRJ1_MYCMM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. 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 EMBL ACC39303.1
Ordered Locus Names:MMAR_0842
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length473 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
B2HRJ1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: B0D498CB9E3453E5

FASTA47349,197
        10         20         30         40         50         60 
MSILLFGVSH RSAPVSVLEQ LSIDESEQVK IVDRVLQSPL VTEAMVLSTC NRVEVYAVVE 

        70         80         90        100        110        120 
AFHGGLSAIG QVLSDHSGMS MGELTKHAYV RYSEAAVEHL FAVASGLDSA VVGEQQVLGQ 

       130        140        150        160        170        180 
VRRSYSAAEA NRTVGRVLHE LAQRALSVGK RVHSETSIDA AGASVVSVAL GIAERKLGGL 

       190        200        210        220        230        240 
GAKTAVVIGA GSMGALSSAH LTRAGIGKVH VLNRSLARAQ RLAGKIRQSG VLAEARTLDR 

       250        260        270        280        290        300 
LAEVLTDADV VVSCTGAVAP VVSLADVHHA LATARRDETT RPLVICDLGM PRDVDPAVAG 

       310        320        330        340        350        360 
LPGVWLIDVE RVQREPSAHA ASADVAAARH IVAAEVAGYL AGQRMAEVTP TVTALRQRAA 

       370        380        390        400        410        420 
DVVEAELLRL DNRLPGLDSA ERDEVARTVR RVVDKLLHAP TVRIKQLASA PGGDSYAEAL 

       430        440        450        460        470 
RELFQLDQTA VDAVATAGEL PVFSSGLDAG AGPQGADGPS AGPTPSAPNP SAE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000854 Genomic DNA. Translation: ACC39303.1.
RefSeqYP_001849158.1. NC_010612.1.

3D structure databases

ProteinModelPortalB2HRJ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2HRJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000032666; EBMYCP00000031106; EBMYCG00000032661.
GeneID6225093.
GenomeReviewsGene locus MMAR_0842 in contig CP000854_GR.
KEGGmmi:MMAR_0842.
PATRIC18062419. VBIMycMar75906_0902.

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.
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 nameB2HRJ1_MYCMM
AccessionPrimary (citable) accession number: B2HRJ1
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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