Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A7HBF2 (HEM12_ANADF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:Anae109_1845
OrganismAnaeromyxobacter sp. (strain Fw109-5) [Complete proteome] [HAMAP]
Taxonomic identifier404589 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length423 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.

Sequence caution

The sequence ABS26048.1 differs from that shown. Reason: Erroneous initiation.

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 – 423423Glutamyl-tRNA reductase 2 HAMAP-Rule MF_00087
PRO_0000335008

Regions

Nucleotide binding183 – 1886NADP By similarity
Region48 – 514Substrate binding By similarity
Region108 – 1103Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site1031Substrate By similarity
Binding site1141Substrate By similarity
Site931Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A7HBF2 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 494272D1FBFC0093

FASTA42345,130
        10         20         30         40         50         60 
MLVAVGLNQK GATVADREVL ALPAEGFQST LAEYAALDAV DEIAVMSTCY RVEIYAATRC 

        70         80         90        100        110        120 
PAAATLSLRQ ALNARAGREL PLFELHGEEA YRHLVRVASS LESAILGEPQ ILGQVKEAFQ 

       130        140        150        160        170        180 
RSIDQGVAAK ELTSVLNRAL SAAKRVRTDT AIGRAGISWG HAAATLAEKV LGKMQGRRVV 

       190        200        210        220        230        240 
VVGAGEMARL SAQHLRDQGA RIVVLNRTLV NGEALAREVG GVARPLEALG EELAQADVVV 

       250        260        270        280        290        300 
SAAPVAPDAF QPEAMAELSR SRKRPIVLVD LAVPRAIPAA TGAIRDVYLC DVDDLDRVMK 

       310        320        330        340        350        360 
AAMSERAAAV ADADRIIAEE VGKFVRAEAE RRAAPLIQEM RTRASAIARE EVERTLRRLG 

       370        380        390        400        410        420 
EDPEVERRLE AMAGSIVSKI LHAPSARLRQ AVCDGCSGEA LVSAAVEIFE LSADIRVHRG 


NAA 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. Fw109-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Fields M., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fw109-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000769 Genomic DNA. Translation: ABS26048.1. Different initiation.
RefSeqYP_001379032.1. NC_009675.1.

3D structure databases

ProteinModelPortalA7HBF2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING404589.Anae109_1845.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS26048; ABS26048; Anae109_1845.
GeneID5377847.
KEGGafw:Anae109_1845.
PATRIC20928931. VBIAnaSp113478_1943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycASP404589:GHMT-1856-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_ANADF
AccessionPrimary (citable) accession number: A7HBF2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 57 of the entry and version 2 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