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Q2IKT3 (HEM12_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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 2

Short name=GluTR 2
EC=1.2.1.70
Gene names
Name:hemA2
Ordered Locus Names:Adeh_2493
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length446 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

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 processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen 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 – 446446Glutamyl-tRNA reductase 2 HAMAP-Rule MF_00087
PRO_0000335006

Regions

Nucleotide binding185 – 1906NADP By similarity
Region53 – 564Substrate binding By similarity
Region110 – 1123Substrate binding By similarity

Sites

Active site541Nucleophile By similarity
Binding site1051Substrate By similarity
Binding site1161Substrate By similarity
Site951Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IKT3 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: B9DFB64DC19CB09C

FASTA44647,370
        10         20         30         40         50         60 
MTGDRRLFLV GLSHKSAPID VRERVALTGD ALKAALCELK AMEGVTEALV VSTCNRVEVF 

        70         80         90        100        110        120 
VHSDRPDAAR RFFTERSPAA ADHLYAKDGV EAVRHLFRVA SSLDSMVVGE QQILGQVKEA 

       130        140        150        160        170        180 
YGLASAASAA GSYFSRLCNR AFATAKRVRT ETEIGRGATS MSQVAVELVE KIFGRLEGRA 

       190        200        210        220        230        240 
ILLVGAGKMG ALSAKALAVL GADRILVTNR SPERGLALAA QVSGSYRGWE ELQRLLGEAD 

       250        260        270        280        290        300 
VVIVSTGAPT YVVTRESMHA AMKARRRRSI CLIDLAVPRN VDPACAELSD VYAYDVDDME 

       310        320        330        340        350        360 
RVVATSKQAR QGEAIRAEAI VEAEVMAFAK EREARAALPV LAQLRRHAER IARAEAERTL 

       370        380        390        400        410        420 
AQVGGKLDDK GRKSVEAMAQ AIVNKLLHGP TSRLKEAASS GDSALPGAAA ELFGIENETA 

       430        440 
GGERREGGAE GAAAAPGAGP VRSQGT 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC82263.1.
RefSeqYP_465700.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IKT3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290397.Adeh_2493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC82263; ABC82263; Adeh_2493.
GeneID3890055.
KEGGade:Adeh_2493.
PATRIC20921161. VBIAnaDeh31384_2558.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAKMLHGTM.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycADEH290397:GI2Z-2524-MONOMER.
UniPathwayUPA00251; UER00316.

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.
IPR018214. Pyrrol_synth_GluRdtase_CS.
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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM12_ANADE
AccessionPrimary (citable) accession number: Q2IKT3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 73 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