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A7ZD34 (HEM1_CAMC1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Ccon26_08200
ORF Names:CCC13826_1051
OrganismCampylobacter concisus (strain 13826) [Complete proteome] [HAMAP]
Taxonomic identifier360104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length427 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 – 427427Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000071246

Regions

Nucleotide binding190 – 1956NADP By similarity
Region50 – 534Substrate binding By similarity
Region115 – 1173Substrate binding By similarity

Sites

Active site511Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site1211Substrate By similarity
Site1001Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZD34 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 618EE0892BDB953A

FASTA42747,802
        10         20         30         40         50         60 
MHYLDISFTY KNTDISVREK LAFDSDEKKE QILKLINSNK NIKESMVLNT CNRVEIIASV 

        70         80         90        100        110        120 
EDVKAATAHI IRCMSIFSGV FEDELYERAD IYENSGAAHH LFAVASSLDS LVVGETQIVG 

       130        140        150        160        170        180 
QLKNAFKFAY DNNSCGEDIS KIIHYACKCA AKVRNETQIS KNPISVSSVA VAKAKEIFGT 

       190        200        210        220        230        240 
LEGKTAIVVG AGEMGELAAK HLISSGAEVI IINRSSERVE QLVDSLGDNA SWDSILKLKE 

       250        260        270        280        290        300 
YVNNYDLIFS STAAPHAIIT GEIIEPREFH RYFFDIAVPR DIDLLNTELI SVYTVDSLEE 

       310        320        330        340        350        360 
IVRKNLALRE EQAQKAYSIV GQDTSEFLKT LKEDMSVPLI KSIRKQAEIC AKNELEKAIK 

       370        380        390        400        410        420 
KGYLKHSDYD EAQKLIHQVF KAFLHQPTMK LKGLADEERA SELSNGVKFL FDIKDEQNFQ 


AGDIDEI 

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References

[1]"Genome sequence of Campylobacter concisus 13826 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., On S., Nelson K.E.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13826.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000792 Genomic DNA. Translation: EAT97817.1.
RefSeqYP_001466692.1. NC_009802.1.

3D structure databases

ProteinModelPortalA7ZD34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360104.CCC13826_1051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAT97817; EAT97817; CCC13826_1051.
GeneID5595979.
KEGGcco:CCC13826_1051.
PATRIC20027839. VBICamCon95352_0862.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMALNKQFET.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCCON360104:GHAC-869-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_CAMC1
AccessionPrimary (citable) accession number: A7ZD34
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 54 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