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B9MRJ1 (HEM1_CALBD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:Athe_1195
OrganismCaldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum) [Complete proteome] [HAMAP]
Taxonomic identifier521460 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length394 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 – 394394Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000118464

Regions

Nucleotide binding175 – 1806NADP By similarity
Region45 – 484Substrate binding By similarity
Region104 – 1063Substrate binding By similarity

Sites

Active site461Nucleophile By similarity
Binding site991Substrate By similarity
Binding site1101Substrate By similarity
Site891Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B9MRJ1 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 7DAA5CDFD6FBFF2A

FASTA39446,380
        10         20         30         40         50         60 
MLWVIGINHK VEVDIRQKFS LIKTKLQEKL ISLKKLANEV IILSTCNRTE IYFFSEEYVD 

        70         80         90        100        110        120 
IEKIFTELDW DKRYMHLFYI YKDKDCIKHL FEVVCGFDSL LIGEDQIVAQ VKEAKEISKL 

       130        140        150        160        170        180 
VGGKNPVLER LFEVALKCSK EFRTKARLNE HPITIASVVG KVLKESNIRK IAIIGLGNIG 

       190        200        210        220        230        240 
ILFCNYFKNS DVDKVFLIGR KNEKIDQFVK LNPEKFRYYD KKKTILEAQC LICSTSAPHS 

       250        260        270        280        290        300 
VVHKDDIPEG KNLLIFDLAV PRDVDVEVYE LPNVKVIDID QVHKIDTINR EFRISKMQEN 

       310        320        330        340        350        360 
YHIIDKYVDE FIDWLEFRQY RNLIMEMKRH AEQLCKAQVK YIKNVDSRER KEVERLLIRM 

       370        380        390 
ANLYIDRAIE VLREAHKEGS GEICSNLIKR IFLK 

« Hide

References

[1]"Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1888 / DSM 6725 / Z-1320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001393 Genomic DNA. Translation: ACM60295.1.
RefSeqYP_002573068.1. NC_012034.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521460.Athe_1195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM60295; ACM60295; Athe_1195.
GeneID7409669.
KEGGate:Athe_1195.
PATRIC20899500. VBIAnaThe135187_1263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000090159.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCBES521460:GH8H-1214-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 nameHEM1_CALBD
AccessionPrimary (citable) accession number: B9MRJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 47 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