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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541NucleophileUniRule annotation
Sitei101 – 1011Important for activityUniRule annotation
Binding sitei111 – 1111SubstrateUniRule annotation
Binding sitei122 – 1221SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBPAR257311:BPP0381-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:BPP0381
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001421 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Glutamyl-tRNA reductasePRO_0000113998Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi257311.BPP0381.

Structurei

3D structure databases

ProteinModelPortaliQ7WCE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 564Substrate bindingUniRule annotation
Regioni116 – 1183Substrate bindingUniRule annotation

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiGAHSISM.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7WCE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVAVLAFGL NHTSAPVSVR ERVSMPVDLV KPALEGLRAT FGGAVREAAI
60 70 80 90 100
LSTCNRTELY CAAEGQVAEH LPAWLAEHNR LEAAALRPHL YRHQHDDAVR
110 120 130 140 150
HAFRVASGLD SMVLGEPQIL GQMKDAVRAA NEAGALGTLL HQLFQRTFSV
160 170 180 190 200
AKEVRSQTAI GAHSVSMAAA AVRLAERVFG QLEDARTLFI GAGEMIELCA
210 220 230 240 250
THFAAQRPRS MVVANRTIER AETLAGRFSA QTMKLADLTE RLAEFDVIVS
260 270 280 290 300
CTASSLPILG LGMVERATRQ RRHRPMVMID LAVPRDIEPE VGRLDDVYLY
310 320 330 340 350
SVDDLGRLVQ SGTDARRAAV VQAEAIIETR VQGFMHWMQS REVVPVIRDL
360 370 380 390 400
HQAADDVRAA ELERARRMLA RGESPEAVLE QLAHGLTQKY LHGPLAALNR
410 420
SEGDERRQLL AWVPRLFPGR DSRR
Length:424
Mass (Da):46,736
Last modified:October 1, 2003 - v1
Checksum:i3E9540D9435A8A27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640424 Genomic DNA. Translation: CAE35965.1.
RefSeqiNP_882735.1. NC_002928.3.

Genome annotation databases

KEGGibpa:BPP0381.
PATRICi21144344. VBIBorPar43418_0397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640424 Genomic DNA. Translation: CAE35965.1.
RefSeqiNP_882735.1. NC_002928.3.

3D structure databases

ProteinModelPortaliQ7WCE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257311.BPP0381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGibpa:BPP0381.
PATRICi21144344. VBIBorPar43418_0397.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiGAHSISM.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciBPAR257311:BPP0381-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Entry informationi

Entry nameiHEM1_BORPA
AccessioniPrimary (citable) accession number: Q7WCE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: April 1, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.