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Q11Y93 (HEM1_CYTH3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:CHU_0333
OrganismCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]
Taxonomic identifier269798 [NCBI]
Taxonomic lineageBacteriaBacteroidetesCytophagiaCytophagalesCytophagaceaeCytophaga

Protein attributes

Sequence length425 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 – 425425Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335025

Regions

Nucleotide binding191 – 1966NADP By similarity
Region51 – 544Substrate binding By similarity
Region116 – 1183Substrate binding By similarity

Sites

Active site521Nucleophile By similarity
Binding site1111Substrate By similarity
Binding site1221Substrate By similarity
Site1011Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11Y93 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: FFB74CC964E8F1FA

FASTA42548,224
        10         20         30         40         50         60 
MISNFKSISL TYRKAPLEIR ERVALNEAEC KSLMLRIKDF TDTAELLILS TCNRTEIYYT 

        70         80         90        100        110        120 
SNEDYSNDII KLLGVEKNIT GLIQQKEYFE IYNEQADAVL HLFEVGIGLD SQVVGDMQIV 

       130        140        150        160        170        180 
NQVKYAYQWS ADLNLAGPFL HRLMHTIFFT NKRVVQETAF RDGAASVSYA TVELSEELLS 

       190        200        210        220        230        240 
ATPNANILIV GLGEIGADVC RNFKANTSFK NITLTNRSPL KSEALAAECG IEHVPFETLW 

       250        260        270        280        290        300 
EAVAKADLVI SSVAKEEPLF TKEEIQKLSI LSHKYFIDLS VPRSVDARAE ELPGIIVYDI 

       310        320        330        340        350        360 
DHIQNRSNEA LENRLNAIPH VRKIILDSIV EFNEWSKEME VSPTINKLKN ALEQIRKEEL 

       370        380        390        400        410        420 
SRFVKQLSDE EAKKVDEITK SIMQKIIKLP VLQLKAACKR GEAETLIDVL NDLFNLDKQP 


EQIRD 

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References

[1]"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii."
Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J.
Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33406 / NCIMB 9469.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000383 Genomic DNA. Translation: ABG57623.1.
RefSeqYP_676963.1. NC_008255.1.

3D structure databases

ProteinModelPortalQ11Y93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269798.CHU_0333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG57623; ABG57623; CHU_0333.
GeneID4185515.
KEGGchu:CHU_0333.
PATRIC21591493. VBICytHut34013_0324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109637.
KOK02492.
OMAVANGVHR.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCHUT269798:GJ83-343-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.
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_CYTH3
AccessionPrimary (citable) accession number: Q11Y93
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 69 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