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P28462 (HEM1_CHLP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 106. 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:Cpar_0738
OrganismChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327)) [Complete proteome] [HAMAP]
Taxonomic identifier517417 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Ref.2

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. Ref.2

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.

Was shown to bind heme, but the precise role of heme is unclear.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protoporphyrinogen 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 – 426426Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114009

Regions

Nucleotide binding189 – 1946NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Experimental info

Sequence conflict144 – 1452TA → SP in AAC61856. Ref.1
Sequence conflict144 – 1452TA → SP in AAA23112. Ref.1
Sequence conflict191 – 22333GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAC61856. Ref.1
Sequence conflict191 – 22333GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAA23112. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28462 [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: D169328D709EF697

FASTA42648,142
        10         20         30         40         50         60 
MNIISVGVNH KTAPIEIRER IALSEVQNKE FVTDLVSSGL ASEAMVVSTC NRTELYVVPG 

        70         80         90        100        110        120 
MPEVNCDYLK DYIISYKDAR NAVRPEHFFN RFYCGTARHL FEVSSAIDSL VLGEGQILGQ 

       130        140        150        160        170        180 
VKDAYRIAAE VGTAGILLTR LCHTAFSVAK KVKTRTKLME GAVSVSYAAV ELAQKIFSNL 

       190        200        210        220        230        240 
SMKKVLLIGA GETGELAAKH MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH 

       250        260        270        280        290        300 
LHEFDIIITA VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD 

       310        320        330        340        350        360 
IDALKHIIDK NLERRRAELP KVKSIIDEEL IGFGQWINTL KVRPTIVDLQ SKFIEIKEKE 

       370        380        390        400        410        420 
LERYRHKVSE EELKRMEHLT DRILKKILHH PIKMLKAPVD TADNIPSKVN LVRNIFDLEE 


PNQSLQ 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the Chlorobium vibrioforme hemA gene."
Majumdar D., Avissar Y.J., Wyche J.H., Beale S.I.
Arch. Microbiol. 156:281-289(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit."
Srivastava A., Beale S.I.
J. Bacteriol. 187:4444-4450(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO C-TERMINUS, FUNCTION, HEME BINDING, SUBUNIT.
[3]"Complete sequence of Chlorobaculum parvum NCIB 8327."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIB 8327.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96364 Genomic DNA. Translation: AAA23112.1.
AF080069 Genomic DNA. Translation: AAC61856.1.
CP001099 Genomic DNA. Translation: ACF11155.1.
PIRA48359.
RefSeqYP_001998355.1. NC_011027.1.

3D structure databases

ProteinModelPortalP28462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING517417.Cpar_0738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF11155; ACF11155; Cpar_0738.
GeneID6419665.
KEGGcpc:Cpar_0738.
PATRIC21364734. VBIChlPar72705_0737.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAKSNANHV.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCPAR517417:GH95-766-MONOMER.
BRENDA1.2.1.70. 1348.
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_CHLP8
AccessionPrimary (citable) accession number: P28462
Secondary accession number(s): B3QMK2, O87494
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 14, 2008
Last modified: May 14, 2014
This is version 106 of the entry and version 3 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