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Reviewed, UniProtKB/Swiss-Prot Q6HD60 (HEM1_BACHK)

Last modified February 9, 2010. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA reductase
      Short name=GluTR
    EC=1.2.1.70
Gene names
Name: hemA
Ordered Locus Names: BT9727_4199
OrganismBacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]
Taxonomic identifier180856 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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

Pathway

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

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.

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Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

porphyrin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionNADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: HAMAP

shikimate 5-dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Glutamyl-tRNA reductase HAMAP MF_00087
PRO_0000113993

Regions

Nucleotide binding189 – 1946NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q6HD60-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 4BB7F3FC998B0643

FASTA44449,825
        10         20         30         40         50         60 
MHILVVSVNY RTAPVEFREK LTFQAAELER AMTTLQNQKS VLENVIVSTC NRTEIYAVVD 

        70         80         90        100        110        120 
QLHTGRYYIK KFLADWFQLE IEEVAPYLTI FEQDGAIDHL FRVTCGLDSM VVGETQILGQ 

       130        140        150        160        170        180 
IKDSFLEAQQ VKATGTIFNE LFKQVITLAK RAHSETTIGE SAMSVSYAAV ELGKKIFGEL 

       190        200        210        220        230        240 
TDCHVLILGA GKMGELALQN LYGSGARKVT VMNRTLSKAE IMAEKYMGHA KPLSELQCAL 

       250        260        270        280        290        300 
LEADILISST GASDYVITKE MMTKVEKMRS GRPLFMVDIA VPRDIDPAID ELEGSFLYDI 

       310        320        330        340        350        360 
DDLQGVVEAN RAERLKEAEK IQFMIEEEIV LFKTWLSTLG VVPLISALRD KALAIQSETM 

       370        380        390        400        410        420 
ESLERKIPNL SDRERKVISK HTKSIINQLL KDPILVAKEI AAEEGADEKL ALFAKIFDLE 

       430        440 
MEDVESRAEE VEHKRVWTPS VPSL

« Hide

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017355 Genomic DNA. Translation: AAT60849.1.
RefSeqYP_038516.1.

3D structure databases

SMRQ6HD60. Positions 2-399.
ModBaseSearch...

Genome annotation databases

GeneID2855613.
GenomeReviewsGene locus BT9727_4199 in contig AE017355_GR.
KEGGbtk:BT9727_4199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG732626.
OMAGPILNRL.

Enzyme and pathway databases

BioCycBTHU281309:BT9727_4199-MONOMER.

Family and domain databases

HAMAPMF_00087. Glu-tRNA_reductase.
[Tree]
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_C.
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.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHEM1_BACHK
AccessionPrimary (citable) accession number: Q6HD60
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents