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

Q59292 (HEM1_CLOJO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. 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
OrganismClostridium josui
Taxonomic identifier1499 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length515 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) Probable. Ref.1

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114012

Regions

Nucleotide binding206 – 2116NADP By similarity
Region68 – 714Substrate binding By similarity

Sites

Active site691Nucleophile By similarity
Binding site1271Substrate By similarity
Binding site1321Substrate By similarity
Binding site1381Substrate By similarity
Site1171Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59292 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A9769824AA30DC4C

FASTA51558,368
        10         20         30         40         50         60 
MQLGRHNSGS IKKRLEMYIL SIISASLDYK SAAIDIRERF SYTSTRIREI LRRIKAADGV 

        70         80         90        100        110        120 
SGAVLLCTCN RTELYISGDN IENMNPALLL CQLSGEEDHK SLMTLFSIRH DSEAIFHLME 

       130        140        150        160        170        180 
VACGLQSMVL FEDRVITQVK NAAAISREEK TIDSTLETLF RLCITAAKKA KTEIKVKAVP 

       190        200        210        220        230        240 
TSAAERAITE LSKKYCFTDK RILVIGNGEI GRLCCKKLIE LGAEITITLR KYKHGEIIIP 

       250        260        270        280        290        300 
VGCNTIPYDE REEVLPLSDV VISATTSPHF TITYDMIEKL ERKPEIFVDL ALPRDIESSI 

       310        320        330        340        350        360 
SNFTGVELYN LDRFYTDYSV LNQKEVSKIR EIINHFILQF EKWKDYREEA AFTKIPDLHN 

       370        380        390        400        410        420 
DTLYGRFPLF IDLSGKKVLV VGGGEIATRR VKTLLRFGAD IYLVAPHLTS ELQEMLNCKL 

       430        440        450        460        470        480 
INYREGYYES QDIQNMFLVI AATNDRETNH KVYLDAKEKG IQMSIADCRE ECSFYFPAIF 

       490        500        510 
EFDGIVGGLV SQNGDNHSLV KSVAEQIRKI GQATD 

« Hide

References

[1]"Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui."
Fujino E., Fujino T., Karita S., Sakka K., Ohmiya K.
J. Bacteriol. 177:5169-5175(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: FERM P-9684.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28503 Genomic DNA. Translation: BAA05860.1.
PIRI40809.

3D structure databases

ProteinModelPortalQ59292.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
IPR006367. Sirohaem_synthase_N.
[Graphical view]
PfamPF05201. GlutR_N. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMSSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01470. cysG_Nterm. 1 hit.
TIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_CLOJO
AccessionPrimary (citable) accession number: Q59292
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 91 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