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B8G817 (HEM1_CHLAD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase

Short name=GluTR
EC=1.2.1.70
Gene names
Name:hemA
Ordered Locus Names:Cagg_1288
OrganismChloroflexus aggregans (strain MD-66 / DSM 9485) [Complete proteome] [HAMAP]
Taxonomic identifier326427 [NCBI]
Taxonomic lineageBacteriaChloroflexiChloroflexalesChloroflexaceaeChloroflexus

Protein attributes

Sequence length453 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-Rule MF_00087

Catalytic activity

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

Pathway

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

Porphyrin-containing compound metabolism; chlorophyll biosynthesis. HAMAP-Rule MF_00087

Subunit structure

Homodimer By similarity. HAMAP-Rule 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-Rule 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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000190511

Regions

Nucleotide binding193 – 1986NADP By similarity
Region54 – 574Substrate binding By similarity
Region118 – 1203Substrate binding By similarity

Sites

Active site551Nucleophile By similarity
Binding site1131Substrate By similarity
Binding site1241Substrate By similarity
Site1031Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B8G817 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 4D3B325E808BA6CE

FASTA45349,496
        10         20         30         40         50         60 
MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALLQLTQADN GSPPLFTEAV ILSTCNRVEI 

        70         80         90        100        110        120 
YGVANPGTTA QHVVDFLANF HRRPAGSFVH TLYFYQGEAV ARHLCATAAG LRSLVLGEAQ 

       130        140        150        160        170        180 
IQGQVRSAYE AAQRIGSVGS VLHRLFQIAL VAGKRVRHET TIGKGAASVS QAGVELARRR 

       190        200        210        220        230        240 
LGDLRGREVL LIGGGEVSEL AAQNLIANGA DRLTIVNRTS SRAAALAERY GAEMLDFGAL 

       250        260        270        280        290        300 
PEALARADIV ISSTAAPVPI IYRHHIAEAL SHKQRMRACG DCDPPAMLLI DLAVPRDIAA 

       310        320        330        340        350        360 
DVAELPGVYL FTVDDLREVV SHTIELRSAV IDIANQIVEE QVREFSDWLR TQEALPVLTM 

       370        380        390        400        410        420 
LRQRAEEVRN EELTRALRRL HDLSPEQRAV IEGLSRSIVN KLLHPPTRCL REAAAHGQGK 

       430        440        450 
RYATMLAELF NLEHALEHKA GAMGNTELTD RMR 

« Hide

References

[1]"Complete sequence of Chloroflexus aggregans DSM 9485."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MD-66 / DSM 9485.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001337 Genomic DNA. Translation: ACL24196.1.
RefSeqYP_002462632.1. NC_011831.1.

3D structure databases

ProteinModelPortalB8G817.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326427.Cagg_1288.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL24196; ACL24196; Cagg_1288.
GeneID7266274.
KEGGcag:Cagg_1288.
PATRIC21405082. VBIChlAgg85409_1336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMALAHKLTN.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCAGG326427:GHS8-1301-MONOMER.
UniPathwayUPA00251; UER00316.
UPA00668.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEM1_CHLAD
AccessionPrimary (citable) accession number: B8G817
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways